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Conserved domains on  [gi|119571101|gb|EAW50716|]
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GRIP1 associated protein 1, isoform CRA_b [Homo sapiens]

Protein Classification

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]; ...
87-405 2.08e-14

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: 76.90  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  87 ELKWEMEKEEKRLL---WEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRkEA 163
Cdd:COG1196  217 ELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEA---ELEELRLEL-EELELELEEAQAE-EY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 164 DHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQ 243
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEAL 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 324 KAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVE 403
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527

                 ..
gi 119571101 404 EL 405
Cdd:COG1196  528 VL 529
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
301-554 1.68e-05

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   301 EIGQEKEQLTQELQEARKSAEKRKAMLDELA--METLQEKSQHKEELGAVRLRHEKEVLGVRARyerELRELHEDKKRQE 378
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKREYEGYELLK---EKEALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEE 458
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-------NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   459 LQDVRDQLEQAQEERDCHLKTISSLKQEVKDtvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSG 538
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
                          250
                   ....*....|....*.
gi 119571101   539 LEELVLSEMNSPSRTQ 554
Cdd:TIGR02169  393 KLEKLKREINELKREL 408
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
87-405 2.08e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  87 ELKWEMEKEEKRLL---WEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRkEA 163
Cdd:COG1196  217 ELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEA---ELEELRLEL-EELELELEEAQAE-EY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 164 DHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQ 243
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEAL 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 324 KAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVE 403
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527

                 ..
gi 119571101 404 EL 405
Cdd:COG1196  528 VL 529
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
88-417 4.30e-11

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: 66.62  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    88 LKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEkLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEAdHKA 167
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQI-LRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   168 QLARtqkLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAkt 247
Cdd:TIGR02168  310 RLAN---LERQLEELEAQLEELESKLD--------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-- 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   248 qelnmlreqttgLAAELQQQQAEYEDLMGQKDDLNSQLQeslransRLLEQLQEIGQEKEQLTQELQEARKSAEkrKAML 327
Cdd:TIGR02168  377 ------------LEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKKLE--EAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   328 DELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRARYErELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:TIGR02168  436 KELQAE-LEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
                          330
                   ....*....|
gi 119571101   408 QVHSMDGAKG 417
Cdd:TIGR02168  514 NQSGLSGILG 523
PTZ00121 PTZ00121
MAEBL; Provisional
94-646 1.73e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   94 KEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEELQQRKEADHK---AQLA 170
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKA 1350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  171 RTQKLQQELEAANQSlAELRDQRQGERLEHAAALRALQDQVSiQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTqel 250
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--- 1425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  251 nmlREQTTGLAAELQQQQAEYEdlmgQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQELQEARKSAE-KRKAMLDE 329
Cdd:PTZ00121 1426 ---KAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAK 1496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  330 LAMETLQEKSQHKEELGAVRLRHEKevlgvraRYERELRELhEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA-Q 408
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKA-EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeE 1568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  409 VHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKgKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVK 488
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  489 DTvDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDiltnskSRSGLEELVLSEMNSPSRTQTGDSSSISSFSYRE 568
Cdd:PTZ00121 1648 KA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101  569 ILREKESSAVPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 646
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-554 1.68e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   301 EIGQEKEQLTQELQEARKSAEKRKAMLDELA--METLQEKSQHKEELGAVRLRHEKEVLGVRARyerELRELHEDKKRQE 378
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKREYEGYELLK---EKEALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEE 458
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-------NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   459 LQDVRDQLEQAQEERDCHLKTISSLKQEVKDtvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSG 538
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
                          250
                   ....*....|....*.
gi 119571101   539 LEELVLSEMNSPSRTQ 554
Cdd:TIGR02169  393 KLEKLKREINELKREL 408
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
115-417 2.01e-05

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: 48.29  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  115 TSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAElrdqrq 194
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKE---------RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  195 gerlehaaalralqdqvsiqsADAQEQVEGLLAENNALRTSLaaleqiqTAKTQELNMLREQTTGLAAELQQQQAEYEDl 274
Cdd:NF012221 1602 ---------------------TNGQAQRDAILEESRAVTKEL-------TTLAQGLDALDSQATYAGESGDQWRNPFAG- 1652
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  275 mGQKDDLNSQLQEslrANSRLLEQLQEIgqeKEQLTQELQEARKSAEKRkamldelamETLQEKSQHKeelgavrlRHEK 354
Cdd:NF012221 1653 -GLLDRVQEQLDD---AKKISGKQLADA---KQRHVDNQQKVKDAVAKS---------EAGVAQGEQN--------QANA 1708
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571101  355 EVLGVRARYERELRELHEDKKRQEEELR---GQIREEKARTRElETLQQTVEELQAQVHSmdGAKG 417
Cdd:NF012221 1709 EQDIDDAKADAEKRKDDALAKQNEAQQAesdANAAANDAQSRG-EQDASAAENKANQAQA--DAKG 1771
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
93-232 7.00e-05

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 45.32  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   93 EKE-EKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKkqesfcrLQTEKETLFNDSRNKIEELQQRKEADHKAQLAR 171
Cdd:pfam14362 105 EKEiDRELLEIQQEEADAAKAQLAAAYRARLAELEAQIAA-------LDAEIDAAEARLDALQAEARCELDGTPGTGTGV 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  172 ------TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVE---GLLAENNAL 232
Cdd:pfam14362 178 pgdgpvAKTKQAQLDAAQAELAALQAQNDARLAALRAELARLTAERAAARARSQAAIDgddGLLARLEAL 247
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
304-537 2.60e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 304 QEKEQLTQELQEARKSAEKRKAMLDELAmetlQEKSQHKEELGAVRLRhekevlgvRARYERELRELHEDKKRQEEELRG 383
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERR--------IAALARRIRALEQELAALEAELAE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 384 QIREEKARTRELETLQQTVEELQAQVHSMdGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVR 463
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 464 DQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRS 537
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
290-531 1.99e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 290 RANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmetlqEKSQHKEELGAVRLRHEKEVLGVRARYER--EL 367
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE-----EVLREINEISSELPELREELEKLEKEVKEleEL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 368 RELHEDKKRQEEELRGQIREEKARTRELET----LQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQ 443
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEErieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 444 CR-EQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKD-------TVDGQRILEKKGSAALKDLKRQLHLE 515
Cdd:PRK03918 317 SRlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakKEELERLKKRLTGLTPEKLEKELEEL 396
                        250
                 ....*....|....*.
gi 119571101 516 RKRADKLQERLQDILT 531
Cdd:PRK03918 397 EKAKEEIEEEISKITA 412
delta-PiCoV-like_Spike_SD1-2_S1-S2_S2 cd22374
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) ...
223-323 7.77e-03

SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses; This group contains the SD-1 and SD-2 subdomains of the S1 subunit C-terminal domain (C-domain), the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses including Falcon coronavirus UAE-HKU27, Magpie-robin coronavirus HKU18, Sparrow coronavirus HKU17, and Night heron coronavirus HKU19. The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the (C-domain. The S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect the S1 and S2 subunits. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP) and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. In the case of human-infecting coronaviruses such as SARS-CoV-2, HCoV-OC43, MERS-CoV, and HCoV-KU1, the spike protein contains an insertion of (R/K)-(2X)n-(R/K) (furin cleavage motif) at the S1/S2 site, which is absent in SARS-CoV and other SARS-related coronaviruses, as well as Ro-BatCoV HKU9. The region modeled in this cd (SD-1 and SD-2, the S1/S2 cleavage region, and the S2 fusion subunit) plays an essential role in viral entry by initiating fusion of the viral and cellular membranes.


Pssm-ID: 411961 [Multi-domain]  Cd Length: 739  Bit Score: 39.48  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 223 EGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRL------- 295
Cdd:cd22374  395 EGLSQVSGAITTVANALTKIQTVVNSQGQALATLTEQLANNFQAISASIADIYNRLNQLEADAQVDRLITGRLaalnafv 474
                         90       100       110
                 ....*....|....*....|....*....|.
gi 119571101 296 ---LEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:cd22374  475 tqtLSKLAEVRQARQLALDKINECVKSQSSR 505
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
87-405 2.08e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.90  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  87 ELKWEMEKEEKRLL---WEQLQGLESSKQAETSRLQEELAKLSEKLKKKQEsfcRLQTEKETLfNDSRNKIEELQQRkEA 163
Cdd:COG1196  217 ELKEELKELEAELLllkLRELEAELEELEAELEELEAELEELEAELAELEA---ELEELRLEL-EELELELEEAQAE-EY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 164 DHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQ 243
Cdd:COG1196  292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEAL 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 324 KAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVE 403
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527

                 ..
gi 119571101 404 EL 405
Cdd:COG1196  528 VL 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-516 1.52e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 187 AELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQ 266
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 267 QQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmETLQEKSQHKEELG 346
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAE 378
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 347 AVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAqvhsmdgakgwfERRLKEA 426
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE------------EEEALEE 446
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 427 EESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDchlktiSSLKQEVKDTVDGQRILEKKGSAALK 506
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL------LLLEAEADYEGFLEGVKAALLLAGLR 520
                        330
                 ....*....|
gi 119571101 507 DLKRQLHLER 516
Cdd:COG1196  521 GLAGAVAVLI 530
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-615 4.59e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  88 LKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLsEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK------ 161
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEAQAEEYELLAELARLEQDIarleer 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 162 ----EADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLA 237
Cdd:COG1196  311 rrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 238 ALEQIQTAKTQELNmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:COG1196  391 ALRAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 318 KSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRH-------EKEVLGVRARYERELRELHEDKKRQEEEL--RGQIREE 388
Cdd:COG1196  470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQ 549
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 389 KARTRELETLQQTVEELQAQVHS-MDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLE 467
Cdd:COG1196  550 NIVVEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 468 QAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEM 547
Cdd:COG1196  630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119571101 548 NspSRTQTGDSSSISSFSYREILREKESSAVPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQE 615
Cdd:COG1196  710 A--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
158-408 2.50e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 158 QQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEhAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLA 237
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 238 ALEQiqtaktqELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:COG1196  299 RLEQ-------DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 318 KSAEKRKAMLDELAMETLQEKSQhkeelgAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE-LE 396
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRA------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEaLE 445
                        250
                 ....*....|..
gi 119571101 397 TLQQTVEELQAQ 408
Cdd:COG1196  446 EAAEEEAELEEE 457
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
88-417 4.30e-11

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: 66.62  E-value: 4.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    88 LKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEkLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEAdHKA 167
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQI-LRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   168 QLARtqkLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAkt 247
Cdd:TIGR02168  310 RLAN---LERQLEELEAQLEELESKLD--------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-- 376
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   248 qelnmlreqttgLAAELQQQQAEYEDLMGQKDDLNSQLQeslransRLLEQLQEIGQEKEQLTQELQEARKSAEkrKAML 327
Cdd:TIGR02168  377 ------------LEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLEDRRERLQQEIEELLKKLE--EAEL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   328 DELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRARYErELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:TIGR02168  436 KELQAE-LEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
                          330
                   ....*....|
gi 119571101   408 QVHSMDGAKG 417
Cdd:TIGR02168  514 NQSGLSGILG 523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
109-471 1.58e-10

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: 64.69  E-value: 1.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETL--FNDSRNKIEELQQRKEAdhKAQLA-RTQKLQQELEAANQS 185
Cdd:TIGR02168  151 EAKPEERRAIFEEAAGISKYKERRKETERKLERTRENLdrLEDILNELERQLKSLER--QAEKAeRYKELKAELRELELA 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   186 LAELRDQRQGERLEhaaALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQ 265
Cdd:TIGR02168  229 LLVLRLEELREELE---ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   266 QQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmETLQEKSQHKEEL 345
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE-SRLEELEEQLETL 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   346 GAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR-ELETLQQTVEELQAQVHSMDGAKGWFERRLK 424
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALE 464
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 119571101   425 EAEESLQQQQQEQEEALKQcreqhAAELKGKEEELQDVRDQLEQAQE 471
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE-----LAQLQARLDSLERLQENLEGFSE 506
PTZ00121 PTZ00121
MAEBL; Provisional
94-646 1.73e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   94 KEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEELQQRKEADHK---AQLA 170
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKA 1350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  171 RTQKLQQELEAANQSlAELRDQRQGERLEHAAALRALQDQVSiQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTqel 250
Cdd:PTZ00121 1351 EAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--- 1425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  251 nmlREQTTGLAAELQQQQAEYEdlmgQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQELQEARKSAE-KRKAMLDE 329
Cdd:PTZ00121 1426 ---KAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKAEE--AKKKAEEAKKADEAKKKAEEAKKADEaKKKAEEAK 1496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  330 LAMETLQEKSQHKEELGAVRLRHEKevlgvraRYERELRELhEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA-Q 408
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKA-EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeE 1568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  409 VHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKgKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVK 488
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  489 DTvDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDiltnskSRSGLEELVLSEMNSPSRTQTGDSSSISSFSYRE 568
Cdd:PTZ00121 1648 KA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101  569 ILREKESSAVPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 646
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
86-409 3.34e-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: 60.46  E-value: 3.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    86 VELKWEMEKEEKRLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQesfcRLQTEKETLFNDSRNKIEELQQRKEAdH 165
Cdd:TIGR02168  673 LERRREIEELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLR----KELEELSRQISALRKDLARLEAEVEQ-L 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   166 KAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTA 245
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI----EQLKEELKALREALDELRAELTLLNEEAAN 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   246 KTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKrka 325
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE--- 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   326 mldelAMETLQEKSQHKEElgavrLRHEKEvlgvraryerELRELHEDKKRQEEELRGQIREEKARTREL-ETLQQTVEE 404
Cdd:TIGR02168  899 -----LSEELRELESKRSE-----LRRELE----------ELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEA 958

                   ....*
gi 119571101   405 LQAQV 409
Cdd:TIGR02168  959 LENKI 963
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
192-522 5.29e-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: 59.69  E-value: 5.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   192 QRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEY 271
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKI----AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   272 EDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMetlqEKSQHKEELGAVRLR 351
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   352 HEKEVLGVrARYERELRELHEDKKRQEEELrgqireeKARTRELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQ 431
Cdd:TIGR02168  826 LESLERRI-AATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   432 QQQQEQEEALKQCREQHaAELKGKEEELQDVRDQLEQAQEERDchlKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQ 511
Cdd:TIGR02168  898 ELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRID---NLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
                          330
                   ....*....|.
gi 119571101   512 LHLERKRADKL 522
Cdd:TIGR02168  974 LKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
110-325 8.41e-09

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: 57.85  E-value: 8.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 110 SKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAEL 189
Cdd:COG4942   17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 190 RDQRQGERLEHAAALRALQDQVSI-------------QSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQ 256
Cdd:COG4942   96 RAELEAQKEELAELLRALYRLGRQpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 257 TTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKA 325
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-337 1.91e-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: 57.76  E-value: 1.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    87 ELKWEMEKEEKRLlwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEadhk 166
Cdd:TIGR02168  271 ELRLEVSELEEEI--EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE---- 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   167 aqlaRTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAK 246
Cdd:TIGR02168  345 ----KLEELKEELESLEAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   247 TQELNMLREqttglaaelQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAM 326
Cdd:TIGR02168  420 QQEIEELLK---------KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
                          250
                   ....*....|.
gi 119571101   327 LDelAMETLQE 337
Cdd:TIGR02168  491 LD--SLERLQE 499
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
83-531 5.82e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.20  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  83 LAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRlQEELAKLSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQ 159
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEER-REELETLEAEIEDLRETIAETEREREELaeeVRDLRERLEELEE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 160 RKE----------ADHKAQLARTQKLQQELEAANQSLAELRdQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAEN 229
Cdd:PRK02224 294 ERDdllaeaglddADAEAVEARREELEDRDEELRDRLEECR-VAAQAHNEEAESLREDADDLEERAEELREEAAELESEL 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 230 NALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQEsLRANSRLLEQLQEIGQEkeql 309
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE-LEATLRTARERVEEAEA---- 447
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 310 tqeLQEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYER-------------------ELREL 370
Cdd:PRK02224 448 ---LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERaedlveaedrierleerreDLEEL 524
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 371 HEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHSMDGAK----GWFERRLKEAEESLQQQQQEQEEALKqcre 446
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevAELNSKLAELKERIESLERIRTLLAA---- 600
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 447 qhAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGsaalkdlkrqlhlERKRADKLQERL 526
Cdd:PRK02224 601 --IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE-------------DKERAEEYLEQV 665

                 ....*
gi 119571101 527 QDILT 531
Cdd:PRK02224 666 EEKLD 670
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
166-408 8.12e-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: 8.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   166 KAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQ---EQVEGLLAENNALRTSLAALEQI 242
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQE 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   243 QTAKTQELNMLREQTTGLAAELQQQQAEYEDL-----MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEAR 317
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   318 KSAEKRKAMLDELameTLQEKSQHKE-ELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELE 396
Cdd:TIGR02169  833 KEIQELQEQRIDL---KEQIKSIEKEiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
                          250
                   ....*....|..
gi 119571101   397 TLQQTVEELQAQ 408
Cdd:TIGR02169  910 AQIEKKRKRLSE 921
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
91-512 1.17e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  91 EMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEA--DHKAQ 168
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEllEALRA 394
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 169 LARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVsiqsADAQEQVEGLLAENNALRTSLAALEQIQTAKTQ 248
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----EEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 249 ELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRAN---------------------------SRLLEQLQE 301
Cdd:COG1196  471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALllaglrglagavavligveaayeaaleAALAAALQN 550
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 302 IGQEKEQLTQELQEARKSAEKRKAM---LDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQE 378
Cdd:COG1196  551 IVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMDGAKGWFER----------------RLKEAEESLQQQQQEQEEALK 442
Cdd:COG1196  631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAlleaeaeleelaerlaEEELELEEALLAEEEEERELA 710
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 443 QCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKgsaaLKDLKRQL 512
Cdd:COG1196  711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE----LERLEREI 776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
235-473 1.37e-07

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: 54.38  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 235 SLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQ 314
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 315 EARKSAEKRKAMLDELaMETLQEKSQHKEELGAVRLRHEKEVLgVRARYereLRELHEDKKRQEEELRGQIREEKARTRE 394
Cdd:COG4942   94 ELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAALRAE 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 395 LETLQQTVEELQAQVHSmdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEER 473
Cdd:COG4942  169 LEAERAELEALLAELEE--------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
95-409 5.17e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 5.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    95 EEKRLLWEQLQGlESSKQAETSRLQEEL--AKLSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEadhkaqlaRT 172
Cdd:TIGR02169  194 DEKRQQLERLRR-EREKAERYQALLKEKreYEGYELLKEKEA----LERQKEAIERQLASLEEELEKLTE--------EI 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   173 QKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNM 252
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   253 LREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKrkamLDELAM 332
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR----LQEELQ 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   333 ETLQEKSQHKEELGAVRLRH-----EKEVLGVR-ARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQ 406
Cdd:TIGR02169  417 RLSEELADLNAAIAGIEAKIneleeEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496

                   ...
gi 119571101   407 AQV 409
Cdd:TIGR02169  497 AQA 499
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
149-366 1.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  149 DSRNKIEELQQRKeadhkaqlartQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVS--IQSADAQEQVEGLL 226
Cdd:COG4913   607 DNRAKLAALEAEL-----------AELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWdeIDVASAEREIAELE 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  227 AENNALRTSLAALEQiqtaktqelnmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEK 306
Cdd:COG4913   675 AELERLDASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  307 EQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEELGavrlRHEKEVLGVRARYERE 366
Cdd:COG4913   744 RLELRALLEERFAAALGDAVERELRENLEERIDALRARLN----RAEEELERAMRAFNRE 799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-542 2.15e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101     4 LEQENQQLKEGAAGAGVAQAGplVDGELLRLQAENTALQKNVAALQERYGKEAGKFSAVSEgqgdppggpaptvlapmPL 83
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESLEA-----------------EL 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    84 AEVELKWEMEK---EEKRLLWE-------------------------QLQGLESSKQ---------------AETSRLQE 120
Cdd:TIGR02168  361 EELEAELEELEsrlEELEEQLEtlrskvaqlelqiaslnneierleaRLERLEDRRErlqqeieellkkleeAELKELQA 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   121 ELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ--RKEADHKAQLARTQKLQQELEAANQSLAELRDQRQG--- 195
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAaeRELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsg 520
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   196 ------------ERLEHA--AALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTT--- 258
Cdd:TIGR02168  521 ilgvlselisvdEGYEAAieAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegf 600
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   259 -GLAAELQQQQAEYEDLM--------------------------------------------GQKDDLNSQLQESLRANS 293
Cdd:TIGR02168  601 lGVAKDLVKFDPKLRKALsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREIE 680
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   294 RLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHE- 372
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEl 759
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   373 -DKKRQEEELRGQIREEKART-RELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEqeealkqcREQHAA 450
Cdd:TIGR02168  760 eAEIEELEERLEEAEEELAEAeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------LESLER 831
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   451 ELKGKEEELQDVRDQLEQAQEErdchlktISSLKQEVKDTVDGQRILEKKGSAALKD---LKRQLHLERKRADKLQERLQ 527
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSED-------IESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEELR 904
                          650
                   ....*....|....*.
gi 119571101   528 DILT-NSKSRSGLEEL 542
Cdd:TIGR02168  905 ELESkRSELRRELEEL 920
PTZ00121 PTZ00121
MAEBL; Provisional
85-637 2.20e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   85 EVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKL-----SEKLKKKQESFCRLQTEKEtlfNDSRNKIEELQQ 159
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavkkAEEAKKDAEEAKKAEEERN---NEEIRKFEEARM 1262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  160 ----RKEADHKAQLARTQKLQQELEAANQS--LAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALR 233
Cdd:PTZ00121 1263 ahfaRRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  234 TSLAALEQIQTAKTQELNMLREQTTglAAELQQQQAEyedlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAE--AAEKKKEEAK------KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  314 QEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKevlgvrARYERELRELHEDKKRQEEelrgqIREEKARTR 393
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE------AKKAEEAKKKAEEAKKADE-----AKKKAEEAK 1483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  394 ELETLQQTVEELQAQVhsmDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQdvRDQLEQAQEER 473
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKA---DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--ADELKKAEELK 1558
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  474 DChlKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEMNSPSRT 553
Cdd:PTZ00121 1559 KA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  554 QTGDSSSISSFSYREILREKESSAVPARSLSSSPQ-----AQPPRPAELSDEEVAELFQRLAETQQEKwmleEKVKHLEV 628
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkkAEEAKKAEEDEKKAAEALKKEAEEAKKA----EELKKKEA 1712

                  ....*....
gi 119571101  629 SSASMAEDL 637
Cdd:PTZ00121 1713 EEKKKAEEL 1721
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
253-512 4.01e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 4.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   253 LREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAM 332
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   333 ETLQEKSQHKE--------ELGAVRLRHEKEVLGVRARYER------ELRELHEDKKRQEEELRGQIREEKARTRELETL 398
Cdd:TIGR02169  752 EIENVKSELKElearieelEEDLHKLEEALNDLEARLSHSRipeiqaELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   399 QQTVEELQAQVHSMDGAKGWFERRLkeaeeslqqqqqEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLK 478
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEI------------ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
                          250       260       270
                   ....*....|....*....|....*....|....
gi 119571101   479 TISSLKQEVKDTVDGQRILEKKGSAALKDLKRQL 512
Cdd:TIGR02169  900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
182-409 4.70e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 182 ANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSlaaleqiqtaktQELNMLREQTTGLA 261
Cdd:COG3206  158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELE 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 262 AELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLE--QLQEIGQEKEQLTQELQEARksaekrkamldelamETLQEKS 339
Cdd:COG3206  226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS---------------ARYTPNH 290
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 340 ----QHKEELGAVRLRHEKEVLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELETLQQTVEELQAQV 409
Cdd:COG3206  291 pdviALRAQIAALRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
76-525 4.71e-06

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: 49.97  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    76 TVLAPMPLAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKL--KKKQESFCRLQTEKETLFNDSRNK 153
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQIEQQAQRI 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   154 IEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEhaaalralqdqvsiQSADAQEQVEGLLAENNALR 233
Cdd:TIGR00618  313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR--------------DAHEVATSIREISCQQHTLT 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   234 TSLAALEQIQTAKTQELNMLR---EQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLT 310
Cdd:TIGR00618  379 QHIHTLQQQKTTLTQKLQSLCkelDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   311 QELQEARKSAEKRKAMLDELAMETLQEKSQHKEElgavrlrhekevlGVRARYERELRELHEDKKRQEEELRGQIREEKA 390
Cdd:TIGR00618  459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV-------------LARLLELQEEPCPLCGSCIHPNPARQDIDNPGP 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   391 RTRELETLQQTVEELQAQVHSMDGaKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQ 470
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 119571101   471 EERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQER 525
Cdd:TIGR00618  605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER 659
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
148-387 5.59e-06

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.95  E-value: 5.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  148 NDSRNKIE---ELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALR--ALQDQVSIQS-ADAQEQ 221
Cdd:COG3096   842 RQRRSELErelAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELdaAQEAQAFIQQhGKALAQ 921
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  222 VEGLLAennALRTSLAALEQIQTAKTQ---ELNMLREQTTGLAAELQQQQA-EYED---LMGQKDDLNSQLQESLR---- 290
Cdd:COG3096   922 LEPLVA---VLQSDPEQFEQLQADYLQakeQQRRLKQQIFALSEVVQRRPHfSYEDavgLLGENSDLNEKLRARLEqaee 998
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  291 ANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQ---------------EKSQHKEELGAVRLRhEKE 355
Cdd:COG3096   999 ARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElgvqadaeaeerariRRDELHEELSQNRSR-RSQ 1077
                         250       260       270
                  ....*....|....*....|....*....|..
gi 119571101  356 VLGVRARYERELRELHEDKKRQEEELRGQIRE 387
Cdd:COG3096  1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-523 1.21e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  91 EMEKEEKRLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEAdhKAQLA 170
Cdd:COG4717   67 ELNLKELKELEEELKEAEE-KEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEAL--EAELA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 171 RTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQEL 250
Cdd:COG4717  143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 251 NMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDEL 330
Cdd:COG4717  223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 331 AMETLQEKSqHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARtRELETLQQTVEELQAQVH 410
Cdd:COG4717  303 EAEELQALP-ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALLAEAG 380
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 411 SMDGAK-----GWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQ 485
Cdd:COG4717  381 VEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 119571101 486 EVKDTVDGQRILEKKgsAALKDLKRQLHLERKRADKLQ 523
Cdd:COG4717  461 ELEQLEEDGELAELL--QELEELKAELRELAEEWAALK 496
PTZ00121 PTZ00121
MAEBL; Provisional
91-631 1.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   91 EMEKEEKRLLWEQLQGLESSKQAETSRLQEElAKLSEKLKKKQESfcrlqteketlFNDSRNKIEELQQRKEADHKAQLA 170
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEE-ARKAEDARKAEEA-----------RKAEDAKRVEIARKAEDARKAEEA 1169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  171 RTQKLQQELEAANQSLAELRDQ--RQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQ 248
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  249 ELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSrlLEQLQEIgQEKEQLTQELQEARKSAE-KRKAML 327
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE--AKKAEEK-KKADEAKKKAEEAKKADEaKKKAEE 1326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  328 DELAMETLQEKSQHKEELGAVRlRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  408 QVHSMDGAKGwfERRLKEAEESLQQQQQEQEEALKQCREQHAA-ELKGKEEELQDVRDQLEQAQEERDChlktiSSLKQE 486
Cdd:PTZ00121 1406 KADELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKA-----DEAKKK 1478
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  487 VKDTVDGQRILEKKGSAALK-DLKRQLHLERKRADKL----QERLQDILTNSKSRSGLEELVLSEMNSPS---RTQTGDS 558
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKaDEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELK 1558
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571101  559 SSISSFSYREILREKESSAVPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKwmlEEKVKHLEVSSA 631
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---EAKIKAEELKKA 1628
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
301-554 1.68e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   301 EIGQEKEQLTQELQEARKSAEKRKAMLDELA--METLQEKSQHKEELGAVRLRHEKEVLGVRARyerELRELHEDKKRQE 378
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKREYEGYELLK---EKEALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   379 EELRGQIREEKARTRELETLQQTVEELQAQVHSMdgakgwfERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEE 458
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-------NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   459 LQDVRDQLEQAQEERDCHLKTISSLKQEVKDtvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSG 538
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
                          250
                   ....*....|....*.
gi 119571101   539 LEELVLSEMNSPSRTQ 554
Cdd:TIGR02169  393 KLEKLKREINELKREL 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
159-534 1.71e-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: 48.13  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   159 QRKEADHKAQLARTQKLQQELEAANQSLaelrdQRQGERLEHAAALRALQDQVSIQSA-----DAQEQVEGLLAENNALR 233
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAELRELELALLvlrleELREELEELQEELKEAE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   234 TSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   314 QEARKSAEKRKAMLDELAMETLQEKSQHKEElgavrlrhekevlgvraryERELRELHEDKKRQEEELRGQIREEKARTR 393
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEEL-------------------EAELEELESRLEELEEQLETLRSKVAQLEL 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   394 ELETLQQTVEELqaqvhsmdgakgwferrlkeaEES----LQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQLEQA 469
Cdd:TIGR02168  394 QIASLNNEIERL---------------------EARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101   470 QEERDCHLKTISSLKQEVkdtvdgqrileKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSK 534
Cdd:TIGR02168  453 QEELERLEEALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
74-340 1.78e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.13  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   74 APTVLAPMPLAEVELKWEMEKEE------KRLLWEQLQG----LESSKQAETSRLQ-----EELAKLSEKLKKKqesfcr 138
Cdd:PRK10929   14 SWGAYAATAPDEKQITQELEQAKaaktpaQAEIVEALQSalnwLEERKGSLERAKQyqqviDNFPKLSAELRQQ------ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  139 LQTEKETLFNDSRN-KIEELQQRKEADHKAQLARTQKLQQELEAANQ---SLAELRDQRQGERLEHAAALRALQDQVSIQ 214
Cdd:PRK10929   88 LNNERDEPRSVPPNmSTDALEQEILQVSSQLLEKSRQAQQEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  215 SADAQEQVEGLLAENNALRTSLAALE--QIQTAKTQELNMLReqttglaAELQQQQAEYEDLMGQ--KDDLNSQLQE--- 287
Cdd:PRK10929  168 TPLAQAQLTALQAESAALKALVDELElaQLSANNRQELARLR-------SELAKKRSQQLDAYLQalRNQLNSQRQReae 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  288 -SLRANSRLLEQ-------LQEIGQEKEQLTQEL-QEARK----SAEKRKAMLDEL----AMETLQEKSQ 340
Cdd:PRK10929  241 rALESTELLAEQsgdlpksIVAQFKINRELSQALnQQAQRmdliASQQRQAASQTLqvrqALNTLREQSQ 310
mukB PRK04863
chromosome partition protein MukB;
91-409 1.97e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.03  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   91 EMEKEEKRLLwEQLQGLESSKQAETSrLQEELAKLSEKLKKKQESfcRLQTEKETLFNDSRNKIEE-LQQRKEADHKAQL 169
Cdd:PRK04863  301 QLAAEQYRLV-EMARELAELNEAESD-LEQDYQAASDHLNLVQTA--LRQQEKIERYQADLEELEErLEEQNEVVEEADE 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  170 ARTQkLQQELEAANQSLAELRDQ----RQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENnaLRTSLAALEQIQTA 245
Cdd:PRK04863  377 QQEE-NEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN--AEDWLEEFQAKEQE 453
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  246 KTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLN-SQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRK 324
Cdd:PRK04863  454 ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ 533
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  325 A---MLDELAMEtLQEKSQHKEELGAVRLRHEKEVLGVRArYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQT 401
Cdd:PRK04863  534 RaerLLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDA 611

                  ....*...
gi 119571101  402 VEELQAQV 409
Cdd:PRK04863  612 LARLREQS 619
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
115-417 2.01e-05

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: 48.29  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  115 TSRLQEELAKLSEKLKKKQESFCRLQTEKetlfndsrnKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAElrdqrq 194
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKE---------RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  195 gerlehaaalralqdqvsiqsADAQEQVEGLLAENNALRTSLaaleqiqTAKTQELNMLREQTTGLAAELQQQQAEYEDl 274
Cdd:NF012221 1602 ---------------------TNGQAQRDAILEESRAVTKEL-------TTLAQGLDALDSQATYAGESGDQWRNPFAG- 1652
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  275 mGQKDDLNSQLQEslrANSRLLEQLQEIgqeKEQLTQELQEARKSAEKRkamldelamETLQEKSQHKeelgavrlRHEK 354
Cdd:NF012221 1653 -GLLDRVQEQLDD---AKKISGKQLADA---KQRHVDNQQKVKDAVAKS---------EAGVAQGEQN--------QANA 1708
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571101  355 EVLGVRARYERELRELHEDKKRQEEELR---GQIREEKARTRElETLQQTVEELQAQVHSmdGAKG 417
Cdd:NF012221 1709 EQDIDDAKADAEKRKDDALAKQNEAQQAesdANAAANDAQSRG-EQDASAAENKANQAQA--DAKG 1771
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
120-318 2.06e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  120 EELAKLSEKLKKKQESFCRLQTEKETL--FNDSR--NKIEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQ- 194
Cdd:COG4913   255 EPIRELAERYAAARERLAELEYLRAALrlWFAQRrlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRg 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  195 --GERLEHAAAlralqdqvsiQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYE 272
Cdd:COG4913   335 ngGDRLEQLER----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 119571101  273 DlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARK 318
Cdd:COG4913   405 E---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
85-527 2.11e-05

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: 48.04  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    85 EVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieELQQRKEAD 164
Cdd:TIGR00618  191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ---------EEQLKKQQL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   165 HKAQLARTQKLQQELEAANQSLAELRDQRQGERL-EHAAALRALQDQVSIQSADAQEQvEGLLAENNALRTSLAALEQIQ 243
Cdd:TIGR00618  262 LKQLRARIEELRAQEAVLEETQERINRARKAAPLaAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   244 TAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNS--QLQESLRAnsrLLEQLQEIGQEKEQLTQEL-QEARKSA 320
Cdd:TIGR00618  341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQKTT---LTQKLQSLCKELDILQREQaTIDTRTS 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   321 EKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQ 400
Cdd:TIGR00618  418 AFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   401 TVEELQ----------AQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCRE--QHAAELKGKEEELQDVRDQLEQ 468
Cdd:TIGR00618  498 ELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSerKQRASLKEQMQEIQQSFSILTQ 577
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101   469 AQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQ 527
Cdd:TIGR00618  578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
83-412 6.56e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  83 LAEVELKWEMEKEEKRLLWEQLQGLESsKQAETSRLQEELAKLSEKLKKKQESFCRLQ----TEKETLFNDSRNKIEELQ 158
Cdd:COG4717  127 LLPLYQELEALEAELAELPERLEELEE-RLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQ 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 159 QRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTS--- 235
Cdd:COG4717  206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgl 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 236 LAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQE 315
Cdd:COG4717  286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 316 ARkSAEKRKAMLDELAMETLQEKSQHKEELGAvRLRHEKEVLGVRARYERELRELHE-----DKKRQEEELRGQIREEKA 390
Cdd:COG4717  366 EE-LEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEllealDEEELEEELEELEEELEE 443
                        330       340
                 ....*....|....*....|..
gi 119571101 391 RTRELETLQQTVEELQAQVHSM 412
Cdd:COG4717  444 LEEELEELREELAELEAELEQL 465
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
93-232 7.00e-05

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 45.32  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   93 EKE-EKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKkqesfcrLQTEKETLFNDSRNKIEELQQRKEADHKAQLAR 171
Cdd:pfam14362 105 EKEiDRELLEIQQEEADAAKAQLAAAYRARLAELEAQIAA-------LDAEIDAAEARLDALQAEARCELDGTPGTGTGV 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  172 ------TQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVE---GLLAENNAL 232
Cdd:pfam14362 178 pgdgpvAKTKQAQLDAAQAELAALQAQNDARLAALRAELARLTAERAAARARSQAAIDgddGLLARLEAL 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-312 7.46e-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: 7.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101     2 EQLEQENQQLKEGAAGAGVaqagplVDGELLRLQAENTALQKNVAALQERYGKEAGKFSAVSEGQGDppggpaptvlapm 81
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES------------- 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    82 pLAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqrk 161
Cdd:TIGR02168  829 -LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR--- 904
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   162 EADHKAQlartqKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:TIGR02168  905 ELESKRS-----ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101   242 iQTAKTQELNMLREQttglaaelqqqqaEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQE 312
Cdd:TIGR02168  980 -KIKELGPVNLAAIE-------------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
PRK11281 PRK11281
mechanosensitive channel MscK;
148-316 1.03e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 45.67  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  148 NDSRNKIEELQQRK--EADHKA-----------------QLARTQKLQQELEAANQSLAElrDQRQGERLEHAAA----- 203
Cdd:PRK11281   39 ADVQAQLDALNKQKllEAEDKLvqqdleqtlalldkidrQKEETEQLKQQLAQAPAKLRQ--AQAELEALKDDNDeetre 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  204 ------LRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTA------KTQELN-MLREQTTG---LAAELQQQ 267
Cdd:PRK11281  117 tlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyansqRLQQIRnLLKGGKVGgkaLRPSQRVL 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101  268 -QAEYEDLMGQkddlNSQLQESLRANSrlleQLQEIGQEK-----------EQLTQELQEA 316
Cdd:PRK11281  197 lQAEQALLNAQ----NDLQRKSLEGNT----QLQDLLQKQrdyltariqrlEHQLQLLQEA 249
46 PHA02562
endonuclease subunit; Provisional
153-371 1.06e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.39  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 153 KIEEL-QQRKEADHKA-----QLARTQKLQQELEAAN-QSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGL 225
Cdd:PHA02562 175 KIRELnQQIQTLDMKIdhiqqQIKTYNKNIEEQRKKNgENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 226 LAENNALRTSLAALE-QIQTAK---------------TQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESL 289
Cdd:PHA02562 254 SAALNKLNTAAAKIKsKIEQFQkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 290 RANSRLLEQLQEIGQEKeqltQELQEARKSAEKRKAMLDELAMETLqeksQHKEELGAVRlRHEKEVLGVRARYERELRE 369
Cdd:PHA02562 334 EQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFV----DNAEELAKLQ-DELDKIVKTKSELVKEKYH 404

                 ..
gi 119571101 370 LH 371
Cdd:PHA02562 405 RG 406
mukB PRK04863
chromosome partition protein MukB;
112-427 1.27e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  112 QAETSRLQEELAKLSEKLKKKQ---ESFCRL---------QTEKETLFNDSRNKIEELQqRKEADHKAQlarTQKLQQEL 179
Cdd:PRK04863  792 RAEREELAERYATLSFDVQKLQrlhQAFSRFigshlavafEADPEAELRQLNRRRVELE-RALADHESQ---EQQQRSQL 867
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  180 EAANQSLAELR----------DQRQGERLEHAAA--LRALQDQVSIQSADAQ-EQVEGLLAennALRTSLAALEQIQTAK 246
Cdd:PRK04863  868 EQAKEGLSALNrllprlnllaDETLADRVEEIREqlDEAEEAKRFVQQHGNAlAQLEPIVS---VLQSDPEQFEQLKQDY 944
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  247 TQELNMLREQTTGLAA--ELQQQQAE--YED---LMGQKDDLNSQLQESLR----ANSRLLEQLQEIGQEKEQLTQELQE 315
Cdd:PRK04863  945 QQAQQTQRDAKQQAFAltEVVQRRAHfsYEDaaeMLAKNSDLNEKLRQRLEqaeqERTRAREQLRQAQAQLAQYNQVLAS 1024
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  316 ARKSAEKRKAMLDELametlqeksqhKEELGAvrlrhekevLGVRARYERELRelhedKKRQEEELRGQIREEKARTREL 395
Cdd:PRK04863 1025 LKSSYDAKRQMLQEL-----------KQELQD---------LGVPADSGAEER-----ARARRDELHARLSANRSRRNQL 1079
                         330       340       350
                  ....*....|....*....|....*....|..
gi 119571101  396 ETlQQTVEELQaqvhsMDGAkgwfERRLKEAE 427
Cdd:PRK04863 1080 EK-QLTFCEAE-----MDNL----TKKLRKLE 1101
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
304-537 2.60e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 304 QEKEQLTQELQEARKSAEKRKAMLDELAmetlQEKSQHKEELGAVRLRhekevlgvRARYERELRELHEDKKRQEEELRG 383
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERR--------IAALARRIRALEQELAALEAELAE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 384 QIREEKARTRELETLQQTVEELQAQVHSMdGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVR 463
Cdd:COG4942   88 LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 464 DQLEQAQEERDCHLKTISSLKQEVKDTVDGQRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRS 537
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
154-355 2.68e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 154 IEELQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALR 233
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 234 TSLAALEQIQtaKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQEL 313
Cdd:COG4717  123 KLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDL 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119571101 314 QEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKE 355
Cdd:COG4717  198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
110-308 3.99e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 110 SKQAETSR----LQEELAKLSEKLKKKQESFCRLQTEKETL-----FNDSRNKIEELQQRK---EADHKAQLARTQKLQQ 177
Cdd:COG3206  168 LRREEARKalefLEEQLPELRKELEEAEAALEEFRQKNGLVdlseeAKLLLQQLSELESQLaeaRAELAEAEARLAALRA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 178 ELEAANQSLAEL-RDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAA-LEQIQTAKTQELNMLRE 255
Cdd:COG3206  248 QLGSGPDALPELlQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQA 327
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 256 QTTGLAAELQQQQAEYEDLMGQKDDLNsQLQESLRANSR----LLEQLQEIGQEKEQ 308
Cdd:COG3206  328 REASLQAQLAQLEARLAELPELEAELR-RLEREVEVARElyesLLQRLEEARLAEAL 383
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
87-394 4.25e-04

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: 43.81  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101    87 ELKWEMEKEEKRLLWEQLQGLESSKQAETSRL--QEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK--- 161
Cdd:pfam02463  709 KEELKKLKLEAEELLADRVQEAQDKINEELKLlkQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkv 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   162 EADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:pfam02463  789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   242 IQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAE 321
Cdd:pfam02463  869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571101   322 KRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRE 394
Cdd:pfam02463  949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
137-407 4.53e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 137 CRLQTEK-ETLFNDSRNKIEELQQRKEA--DHKAQLARTQKLQQELEAANQSLAELRDqRQGERLEHAAALRALQDQVSI 213
Cdd:PRK02224 473 DRERVEElEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRE-TIEEKRERAEELRERAAELEA 551
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 214 QSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREqttglaaeLQQQQAEYEDLMGQKDDLNSQLQESLRANS 293
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELND 623
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 294 RLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEElgaVRLRHEKEVLGVraryERELRELhed 373
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE---ERDDLQAEIGAV----ENELEEL--- 693
                        250       260       270
                 ....*....|....*....|....*....|....
gi 119571101 374 kkrqeEELRGQIREEKARTRELETLQQTVEELQA 407
Cdd:PRK02224 694 -----EELRERREALENRVEALEALYDEAEELES 722
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
117-410 5.97e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.40  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  117 RLQEELAKLSEKLkkkqesfcRLQTEKETLFNDSRNKIEELQQRKEADH---KAQLArtqKLQQELEA----ANQSLAEL 189
Cdd:COG3096   351 RYQEDLEELTERL--------EEQEEVVEEAAEQLAEAEARLEAAEEEVdslKSQLA---DYQQALDVqqtrAIQYQQAV 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  190 RDQRQGERLEHAAALRA--LQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNML----REQTTGLAAE 263
Cdd:COG3096   420 QALEKARALCGLPDLTPenAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAgeveRSQAWQTARE 499
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  264 LQQQQAEYEDLMGQKDDLNSQLQEslransrlLEQLQEIGQEKEQLTQELQearKSAEKRKAMLDELAMetlqeksqHKE 343
Cdd:COG3096   500 LLRRYRSQQALAQRLQQLRAQLAE--------LEQRLRQQQNAERLLEEFC---QRIGQQLDAAEELEE--------LLA 560
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101  344 ELGAVRLRHEKEVlgvraryeRELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVH 410
Cdd:COG3096   561 ELEAQLEELEEQA--------AEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSG 619
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
139-542 6.04e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.18  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   139 LQTEKETLFNDSRNKIEELQQRKEAdhkaqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADA 218
Cdd:pfam15921  243 VEDQLEALKSESQNKIELLLQQHQD-------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   219 QEQVEGLLAENNALRTSLAALEQIQTAKTQElnmLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLranSRLLEQ 298
Cdd:pfam15921  316 MRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKR 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   299 LQEIGQEKEQ---LTQELQEARKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYE--RELRELHED 373
Cdd:pfam15921  390 EKELSLEKEQnkrLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQ 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   374 KKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHSmdgakgwferrlKEAEESLQQQQQEQEEALKQCREQHAAELK 453
Cdd:pfam15921  470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE------------KERAIEATNAEITKLRSRVDLKLQELQHLK 537
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   454 GKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKDTVdgqRILEKKGSAALKDLKRQLHLERKRADKLQERLQDILTNS 533
Cdd:pfam15921  538 NEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT---QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614

                   ....*....
gi 119571101   534 KSRSGLEEL 542
Cdd:pfam15921  615 KKDAKIREL 623
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
290-531 1.99e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 290 RANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAmetlqEKSQHKEELGAVRLRHEKEVLGVRARYER--EL 367
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE-----EVLREINEISSELPELREELEKLEKEVKEleEL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 368 RELHEDKKRQEEELRGQIREEKARTRELET----LQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQ 443
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEErieeLKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 444 CR-EQHAAELKGKEEELQDVRDQLEQAQEERDCHLKTISSLKQEVKD-------TVDGQRILEKKGSAALKDLKRQLHLE 515
Cdd:PRK03918 317 SRlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakKEELERLKKRLTGLTPEKLEKELEEL 396
                        250
                 ....*....|....*.
gi 119571101 516 RKRADKLQERLQDILT 531
Cdd:PRK03918 397 EKAKEEIEEEISKITA 412
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-424 3.19e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 260 LAAELQQQQAEYEDLMGQKDDLNSQ----LQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDEL----- 330
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPELNLKelkeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllq 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 331 AMETLQEKSQHKEELGAV--RLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR-ELETLQQTVEELQA 407
Cdd:COG4717  127 LLPLYQELEALEAELAELpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206
                        170
                 ....*....|....*..
gi 119571101 408 QVHSMDGAKGWFERRLK 424
Cdd:COG4717  207 RLAELEEELEEAQEELE 223
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
193-337 3.32e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.22  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 193 RQGERLEHAAALRALQDQVsiqsADAQEQVEglLAENNaLRTSLAALEQIQTAK-----TQELNMLREQTTGLAAELQQQ 267
Cdd:COG3524  161 AESEELVNQLSERAREDAV----RFAEEEVE--RAEER-LRDAREALLAFRNRNgildpEATAEALLQLIATLEGQLAEL 233
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119571101 268 QAEYEDLMGQKDDLNSQLQeSLRANSRLLEqlQEIGQEKEQLTQELQE---ARKSAEKRKAMLD-ELAMETLQE 337
Cdd:COG3524  234 EAELAALRSYLSPNSPQVR-QLRRRIAALE--KQIAAERARLTGASGGdslASLLAEYERLELErEFAEKAYTS 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
157-387 3.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 157 LQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSL 236
Cdd:COG1196  548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 237 AALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEA 316
Cdd:COG1196  628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571101 317 RKSAEKRKAMLDELAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYERELRELHEDKKRQEEELRGQIRE 387
Cdd:COG1196  708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
PTZ00121 PTZ00121
MAEBL; Provisional
84-329 3.94e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   84 AEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESF-----CRLQTEKETLFNDSRNKIEELQ 158
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVEQLK 1639
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  159 QRKEAD-HKAQLARTQKLQQELEAANQSLAELRDQRQGERL---EHAAALRALQDQVSIQSADAQEQVEGLLAENNALRT 234
Cdd:PTZ00121 1640 KKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  235 SLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEqlQEIGQEKEQLTQELQ 314
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--EELDEEDEKRRMEVD 1797
                         250
                  ....*....|....*
gi 119571101  315 EARKSAEKRKAMLDE 329
Cdd:PTZ00121 1798 KKIKDIFDNFANIIE 1812
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
118-411 4.18e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  118 LQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ--RKEADHKAQLartQKLQQELEAAN-QSLAELRDQRQ 194
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnKKIKELEKQL---NQLKSEISDLNnQKEQDWNKELK 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  195 GERLEHAAALRALQDQVSiqsaDAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDL 274
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIS----QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  275 MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKAMLDELAMETLQEKSQHKeELGAVRLRHEK 354
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESLET 468
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101  355 EVlgvrARYERELRELHEDKKRQEEELRGQIREEKARTRELETLQQTVEELQAQVHS 411
Cdd:TIGR04523 469 QL----KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
102-553 4.25e-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: 40.59  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   102 EQLQGLESSKQAETSRLQEELAKLSEKLKKKQeSFCRLQTEKETLFNDSRNKIEELQQRKEADHKAQLART-----QKLQ 176
Cdd:pfam12128  322 SELEALEDQHGAFLDADIETAAADQEQLPSWQ-SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikDKLA 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   177 QELEAANQSLAELRDQRQGERlehaAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAALEQI---QTAKTQELNML 253
Cdd:pfam12128  401 KIREARDRQLAVAEDDLQALE----SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELllqLENFDERIERA 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   254 REQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQeslRANSRLLEQLQEIGQEKEQLTQE----LQEARKSAEKRKAMLDE 329
Cdd:pfam12128  477 REEQEAANAEVERLQSELRQARKRRDQASEALR---QASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGK 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   330 LAMETLQEKSQHKEELGAVRLRHEKEVLGVRARYER----ELRELHEDKKRQEEELRGQIREEKARTRELET-LQQTVEE 404
Cdd:pfam12128  554 VISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLDKAEEALQSAREKQAAAEEqLVQANGE 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   405 LQAQVHSMDGAKgwfeRRLKEAEESLQQQQQEQEEALKQCREQHAAELKGKEEELQDVRDQL-------EQAQEERDCHL 477
Cdd:pfam12128  634 LEKASREETFAR----TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqldkkhQAWLEEQKEQK 709
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571101   478 KTISSLKQEVKDTVDGQRilekkgSAALKDLKRQLHLERKRADKLQERLQDILTNSKSRSGLEELVLSEMNSPSRT 553
Cdd:pfam12128  710 REARTEKQAYWQVVEGAL------DAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRT 779
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
70-384 4.26e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.13  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   70 PGGPAPTVLAPMPLAEVELKWEMEKEEKrllwEQLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFND 149
Cdd:pfam09731  79 SKEPKEEKKQVKIPRQSGVSSEVAEEEK----EATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDD 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  150 SRNKIEE-LQQRKEADHKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAE 228
Cdd:pfam09731 155 AIQAVKAhTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEK 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  229 NNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQqqAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQeigqekEQ 308
Cdd:pfam09731 235 VEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIP--VLKEDNLLSNDDLNSLIAHAHREIDQLSKKLA------EL 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  309 LTQELQEARKSAEKRKAMLDELAMETLQEKSQHK-EELGAVRLRHEKEVLGVRARYERELR-------ELHEDKKRQEEE 380
Cdd:pfam09731 307 KKREEKHIERALEKQKEELDKLAEELSARLEEVRaADEAQLRLEFEREREEIRESYEEKLRtelerqaEAHEEHLKDVLV 386

                  ....
gi 119571101  381 LRGQ 384
Cdd:pfam09731 387 EQEI 390
PRK09039 PRK09039
peptidoglycan -binding protein;
109-241 4.57e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLfndsrnkieelqqrkeadhKAQLARTQKLQQELEAANQSLAE 188
Cdd:PRK09039  49 SGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANL-------------------RASLSAAEAERSRLQALLAELAG 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119571101 189 LRDQRQGERLEHAAALRALQDQvsiqSADAQEQVEGLLAENNALRTSLAALEQ 241
Cdd:PRK09039 110 AGAAAEGRAGELAQELDSEKQV----SARALAQVELLNQQIAALRRQLAALEA 158
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
83-239 4.59e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101   83 LAEVELKWEMEKEEKRLLWE--QLQGLESSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQR 160
Cdd:COG3096   521 LAELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR 600
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101  161 KEADHKAQlARTQKLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSIQSADAQEQVEGLLAENNALRTSLAAL 239
Cdd:COG3096   601 APAWLAAQ-DALERLREQSGEALADSQEVTAAMQ-QLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLAL 677
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
216-345 5.05e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 216 ADAQEQVEGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYED-----LMGQKDDLNSQLQESLR 290
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedklLEEAEKEAQQAIKEAKK 584
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119571101 291 ANSRLLEQLQEIGQEK--EQLTQELQEARKSAEKRKamldELAMETLQEKSQHKEEL 345
Cdd:PRK00409 585 EADEIIKELRQLQKGGyaSVKAHELIEARKRLNKAN----EKKEKKKKKQKEKQEEL 637
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
109-325 7.72e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 109 SSKQAETSRLQEELAKLSEKLKKKQESFCRLQTEKetlfNDSRNKIEELQQRKEadhkaqlartqKLQQELEAANQSLAE 188
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEID-----------KLQAEIAEAEAEIEE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 189 LRDQRqGERLEHAAALRALQDQVSI--QSADAQEQVEGLLAENNALRTSLAALEQIQTAKtQELNMLREQTTGLAAELQQ 266
Cdd:COG3883   84 RREEL-GERARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119571101 267 QQAEYEDlmgQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKSAEKRKA 325
Cdd:COG3883  162 LKAELEA---AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
delta-PiCoV-like_Spike_SD1-2_S1-S2_S2 cd22374
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) ...
223-323 7.77e-03

SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses; This group contains the SD-1 and SD-2 subdomains of the S1 subunit C-terminal domain (C-domain), the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from Pigeon coronavirus UAE-HKU29, and related avian deltacoronaviruses including Falcon coronavirus UAE-HKU27, Magpie-robin coronavirus HKU18, Sparrow coronavirus HKU17, and Night heron coronavirus HKU19. The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the (C-domain. The S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect the S1 and S2 subunits. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP) and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. In the case of human-infecting coronaviruses such as SARS-CoV-2, HCoV-OC43, MERS-CoV, and HCoV-KU1, the spike protein contains an insertion of (R/K)-(2X)n-(R/K) (furin cleavage motif) at the S1/S2 site, which is absent in SARS-CoV and other SARS-related coronaviruses, as well as Ro-BatCoV HKU9. The region modeled in this cd (SD-1 and SD-2, the S1/S2 cleavage region, and the S2 fusion subunit) plays an essential role in viral entry by initiating fusion of the viral and cellular membranes.


Pssm-ID: 411961 [Multi-domain]  Cd Length: 739  Bit Score: 39.48  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 223 EGLLAENNALRTSLAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRL------- 295
Cdd:cd22374  395 EGLSQVSGAITTVANALTKIQTVVNSQGQALATLTEQLANNFQAISASIADIYNRLNQLEADAQVDRLITGRLaalnafv 474
                         90       100       110
                 ....*....|....*....|....*....|.
gi 119571101 296 ---LEQLQEIGQEKEQLTQELQEARKSAEKR 323
Cdd:cd22374  475 tqtLSKLAEVRQARQLALDKINECVKSQSSR 505
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
240-329 9.00e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  240 EQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQELQEARKS 319
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
                          90
                  ....*....|...
gi 119571101  320 AEKRKAM---LDE 329
Cdd:PRK11448  221 ITDQAAKrleLSE 233
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
83-528 9.39e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 9.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  83 LAEVELKWEMEKEEKRLLWEQLQGLESSKQAETSRLQ--EELAKLSEKLKKKQESFCRLQTEKETlFNDSRNKIEELqqr 160
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKR--- 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 161 kEADHKAQLARTQKLQQELEAANQSLAELRD-----QRQGERLEHAAALRALQDQVSIQSADAQEQVEGLLAENnaLRTS 235
Cdd:PRK03918 316 -LSRLEEEINGIEERIKELEEKEERLEELKKklkelEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKE 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 236 LAALEQIQTAKTQELNMLREQTTGLAAELQQQQAEYEDLMGQKDD---LNSQLQESLRAN--SRLLEQLQEIGQEKEQLT 310
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKEllEEYTAELKRIEKELKEIE 472
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 311 QELQEARKSAEK-RKAMLDELAMETLQEKSQHKEELgavrlrhEKEVLGVRARYERELRELHEDKKRQEEELRGQIREEK 389
Cdd:PRK03918 473 EKERKLRKELRElEKVLKKESELIKLKELAEQLKEL-------EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101 390 ARTRELETLQQTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEALKQCREQH------AAELKGKEEELQDVR 463
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLE 625
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101 464 DQLEQAQEERDCHLKTISSLKQEVKDTvdgQRILEKKGSAALKDLKRQLHLERKRADKLQERLQD 528
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEEL---EKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
231-408 9.67e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.27  E-value: 9.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  231 ALRTSLAALEQIQTA--KTQELNMLREQTTGLAAELQQQQAEYED------LMGQKDDLNsqlQESLRANSRLLEQLQEI 302
Cdd:PRK10929   49 ALQSALNWLEERKGSleRAKQYQQVIDNFPKLSAELRQQLNNERDeprsvpPNMSTDALE---QEILQVSSQLLEKSRQA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571101  303 GQEKE----------QLTQELQEARK---------------------------SAEK--RKAMLDELAMETLQekSQHKE 343
Cdd:PRK10929  126 QQEQDrareisdslsQLPQQQTEARRqlneierrlqtlgtpntplaqaqltalQAESaaLKALVDELELAQLS--ANNRQ 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119571101  344 ELgaVRLRHEkevlgvraRYERElrelHEDKKRQEEELRGQIREEkaRTRELETLQQTVEELQAQ 408
Cdd:PRK10929  204 EL--ARLRSE--------LAKKR----SQQLDAYLQALRNQLNSQ--RQREAERALESTELLAEQ 252
 
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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