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Conserved domains on  [gi|1009411338|gb|KYN30324|]
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Rab11 family-interacting protein 4A [Trachymyrmex cornetzi]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1006538)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-397 1.08e-11

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: 67.27  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 208 LSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREwASRLERERQLQL 287
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 288 EncdiKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAhhmLDVMREELSLR 367
Cdd:COG1196   309 E----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA---EAELAEAEEEL 381

                         170       180       190
                  ....*....|....*....|....*....|
gi 1009411338 368 NEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEA 411
RBD-FIP super family cl09694
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 450-490 9.79e-09

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


The actual alignment was detected with superfamily member pfam09457:

Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 50.80  E-value: 9.79e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1009411338 450 TMAELKQALKEQQEVNSQLRTYIDGILLNIVENYPQLLEVK 490
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-397 1.08e-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: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 208 LSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREwASRLERERQLQL 287
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 288 EncdiKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAhhmLDVMREELSLR 367
Cdd:COG1196   309 E----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA---EAELAEAEEEL 381

                         170       180       190
                  ....*....|....*....|....*....|
gi 1009411338 368 NEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEA 411
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 450-490 9.79e-09

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 50.80  E-value: 9.79e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1009411338 450 TMAELKQALKEQQEVNSQLRTYIDGILLNIVENYPQLLEVK 490
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-387 1.05e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETR-----------------AEERL 265
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltllneeaanLRERL 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  266 QAEQRRHREWASRLERERQlQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERH 345
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1009411338  346 AISRANEAHHMLDVMREELslrNEDQQRLEELVQQVVQLQAR 387
Cdd:TIGR02168  906 LESKRSELRRELEELREKL---AQLELRLEGLEVRIDNLQER 944
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
215-397 1.93e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 215 IQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAE-ERLQAEQ-RRHREWASRLERERQLQLENCDI 292
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAvEARREELEDRDEELRDRLEECRV 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 293 KLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESE---RHAISRANEAHHMLDVMREELSLRNE 369
Cdd:PRK02224  336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeelEEEIEELRERFGDAPVDLGNAEDFLE 415

                         170       180
                  ....*....|....*....|....*....
gi 1009411338 370 D-QQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:PRK02224  416 ElREERDELREREAELEATLRTARERVEE 444
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 251-380 1.26e-05

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 45.08  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 251 EEAAKDAETRAEERLQAEQRRHREWASRLERERQLQLENcDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLR 330
Cdd:pfam07321  12 EDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQE-EQRLYAEIQGKLVLLKELEKVKQQVALLRENEADLEKQVA 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1009411338 331 EARREADAARESERHAISRANEAHHMLDVMREELSLRNED----QQRLEELVQQ 380
Cdd:pfam07321  91 EARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEelrqQERQEEQELE 144
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 294-384 5.87e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 294 LQAAELDNSSLREEIARVREQLETARTDKAQLendLREARREADAARESerhAISRAN-EAHHMLDVMREElsLRNEDQQ 372
Cdd:cd06503    39 LEEAEKAKEEAEELLAEYEEKLAEARAEAQEI---IEEARKEAEKIKEE---ILAEAKeEAERILEQAKAE--IEQEKEK 110

                          90
                  ....*....|..
gi 1009411338 373 RLEELVQQVVQL 384
Cdd:cd06503   111 ALAELRKEVADL 122
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-397 1.08e-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: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 208 LSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREwASRLERERQLQL 287
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 288 EncdiKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAhhmLDVMREELSLR 367
Cdd:COG1196   309 E----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA---EAELAEAEEEL 381

                         170       180       190
                  ....*....|....*....|....*....|
gi 1009411338 368 NEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 199-396 1.18e-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: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 199 DVSLEDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASR 278
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 279 LERERQLQ--LENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHM 356
Cdd:COG1196   385 AEELLEALraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1009411338 357 LDVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRD 396
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
211-393 1.68e-10

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.78  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  211 KVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAEtrAEERLQAEQRRHREWASRLERerqLQLENC 290
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW--DEIDVASAEREIAELEAELER---LDASSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  291 DIKLQAAELDnsSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHH-MLDVMREELSLRNE 369
Cdd:COG4913    686 DLAALEEQLE--ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRaLLEERFAAALGDAV 763

                          170       180
                   ....*....|....*....|....
gi 1009411338  370 DQQRLEELVQQVVQLQARNKSLEE 393
Cdd:COG4913    764 ERELRENLEERIDALRARLNRAEE 787
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 208-397 8.62e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 8.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 208 LSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASRLERERQL-- 285
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELee 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 286 QLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELS 365
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1009411338 366 LRNEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   418 RLEEELEELEEALAELEEEEEEEEEALEEAAE 449
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-379 1.43e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 60.70  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  209 SHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASRLERERQlQLE 288
Cdd:COG4913    287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA-RLE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  289 NcdiKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAAR----------ESERHAISRAN-----EA 353
Cdd:COG4913    366 A---LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelrelEAEIASLERRKsnipaRL 442

                          170       180
                   ....*....|....*....|....*.
gi 1009411338  354 HHMLDVMREELSLRNEDQQRLEELVQ 379
Cdd:COG4913    443 LALRDALAEALGLDEAELPFVGELIE 468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 203-397 4.20e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASRLERE 282
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 283 RQLQ--LENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLRE-ARREADAARESERHAISRANEAHHMLDV 359
Cdd:COG1196   354 EEAEaeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEElEEAEEALLERLERLEEELEELEEALAEL 433

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1009411338 360 MREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 211-414 6.20e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 6.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 211 KVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASRLERERQLQLENC 290
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 291 DIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAAR------ESERHAISRANEAHHMLDVMREEL 364
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeeleELEEALAELEEEEEEEEEALEEAA 448

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009411338 365 SLRNEDQQRLEELVQQVVQLQARNKSLEESRDELQAAAALQAGRELIMLN 414
Cdd:COG1196   449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 450-490 9.79e-09

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 50.80  E-value: 9.79e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1009411338 450 TMAELKQALKEQQEVNSQLRTYIDGILLNIVENYPQLLEVK 490
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
203-393 2.43e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.85  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  203 EDVMDLSHKVQMIQEQMDALADTKSVGEeRYTRAKQENATLHARILMLE----EAAKDAETRAEERLQAEQRRHREWASR 278
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRlwfaQRRLELLEAELEELRAELARLEAELER 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  279 LERERQLQLENCDiKLQAAELDNS-----SLREEIARVREQLETARTDKAQLENDLREARREADAARESerhAISRANEA 353
Cdd:COG4913    314 LEARLDALREELD-ELEAQIRGNGgdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEA 389

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1009411338  354 HHMLDVMREElslRNEDQQRLEELVQQVVQLQARNKSLEE 393
Cdd:COG4913    390 AALLEALEEE---LEALEEALAEAEAALRDLRRELRELEA 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 231-410 3.68e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 231 ERYTRAKQENATLHARILMLE-EAAKDAETRAEERLQAEQRRHREWASRLeRERQLQLENCDIKLQAAELDNSSLREEIA 309
Cdd:COG1196   213 ERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEY 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 310 RVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSLRNEDQQRLEELVQQVVQLQARNK 389
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                         170       180
                  ....*....|....*....|.
gi 1009411338 390 SLEESRDELQAAAALQAGREL 410
Cdd:COG1196   372 AELAEAEEELEELAEELLEAL 392
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-387 1.05e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETR-----------------AEERL 265
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelraeltllneeaanLRERL 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  266 QAEQRRHREWASRLERERQlQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERH 345
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEE-QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1009411338  346 AISRANEAHHMLDVMREELslrNEDQQRLEELVQQVVQLQAR 387
Cdd:TIGR02168  906 LESKRSELRRELEELREKL---AQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 226-393 1.80e-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: 53.92  E-value: 1.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  226 KSVGEERYTRAKQENATLHARIlmleEAAKDAETRAEERLQAEQRRHREWASRLEReRQLQLENCDIKLQAAELDNSSLR 305
Cdd:TIGR02169  282 KDLGEEEQLRVKEKIGELEAEI----ASLERSIAEKERELEDAEERLAKLEAEIDK-LLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  306 EEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSLRNEDQQRLEE----LVQQV 381
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAaiagIEAKI 436

                          170
                   ....*....|..
gi 1009411338  382 VQLQARNKSLEE 393
Cdd:TIGR02169  437 NELEEEKEDKAL 448
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-393 1.90e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  207 DLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWASRLERERQLQ 286
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  287 LEncdikLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARRE-ADAARESERHAISRANEAHHMLDVMREELS 365
Cdd:TIGR02168  379 EQ-----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEiEELLKKLEEAELKELQAELEELEEELEELQ 453

                          170       180
                   ....*....|....*....|....*....
gi 1009411338  366 LRNED-QQRLEELVQQVVQLQARNKSLEE 393
Cdd:TIGR02168  454 EELERlEEALEELREELEEAEQALDAAER 482
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
215-397 1.93e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.89  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 215 IQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAE-ERLQAEQ-RRHREWASRLERERQLQLENCDI 292
Cdd:PRK02224  256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAvEARREELEDRDEELRDRLEECRV 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 293 KLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESE---RHAISRANEAHHMLDVMREELSLRNE 369
Cdd:PRK02224  336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeelEEEIEELRERFGDAPVDLGNAEDFLE 415

                         170       180
                  ....*....|....*....|....*....
gi 1009411338 370 D-QQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:PRK02224  416 ElREERDELREREAELEATLRTARERVEE 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 236-397 2.82e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 236 AKQENATLHARILMLEEAAKDAETRAEERLQAEQRrhREWASRLERERQLQLENCDIKLQAAELDNSSLREEIARVREQL 315
Cdd:COG1196   206 ERQAEKAERYRELKEELKELEAELLLLKLRELEAE--LEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 316 ETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSlrnEDQQRLEELVQQVVQLQARNKSLEESR 395
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE---ELEEELEELEEELEEAEEELEEAEAEL 360


                  ..
gi 1009411338 396 DE 397
Cdd:COG1196   361 AE 362
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
230-381 3.64e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 3.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  230 EERYTRAKQENATLHArilmLEEAAKDAEtRAEERLQAEQRRHREWASRLERERQLQLENCDIKLQAAELDNSSLREEIA 309
Cdd:COG4913    224 FEAADALVEHFDDLER----AHEALEDAR-EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009411338  310 RVREQLETARTDKAQLENDLREARREADAARESER-HAISRANEAHHMLDVMREELSLRNEDQQRLEELVQQV 381
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-397 5.16e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 249 MLEEAA---------KDAETR---AEERL-------------------QAEQ-RRHREWASRL-ERERQLQLencdIKLQ 295
Cdd:COG1196   160 IIEEAAgiskykerkEEAERKleaTEENLerledilgelerqleplerQAEKaERYRELKEELkELEAELLL----LKLR 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 296 AAELDNSSLREEIARV---RE----QLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREElslRN 368
Cdd:COG1196   236 ELEAELEELEAELEELeaeLEeleaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER---RR 312

                         170       180
                  ....*....|....*....|....*....
gi 1009411338 369 EDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEE 341
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 253-397 8.82e-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: 50.92  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 253 AAKDAETRAE-ERLQAEQRRHREWASRLERER---QLQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLEND 328
Cdd:COG4942    19 ADAAAEAEAElEQLQQEIAELEKELAALKKEEkalLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 329 LRE-----ARREADAARESERHAI------SRANEAHHMLDVMReelSLRNEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG4942    99 LEAqkeelAELLRALYRLGRQPPLalllspEDFLDAVRRLQYLK---YLAPARREQAEELRADLAELAALRAELEAERAE 175
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
245-397 8.83e-07

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: 8.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  245 ARILMLEEAAKDAETR---AEERLQAEQRRHREWASRLERERQLQlencdiKLQAAELDNSSLREEIARVREQLETARTD 321
Cdd:COG4913    610 AKLAALEAELAELEEElaeAEERLEALEAELDALQERREALQRLA------EYSWDEIDVASAEREIAELEAELERLDAS 683

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009411338  322 K---AQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG4913    684 SddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
213-393 9.02e-07

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 49.82  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 213 QMIQEQMDALADTKS-----VGEERytRAKQENATLHARILMLEEAAKDAETRAEERLqAeqrrhREWAsrlerERQLQL 287
Cdd:COG1842    30 QAIRDMEEDLVEARQalaqvIANQK--RLERQLEELEAEAEKWEEKARLALEKGREDL-A-----REAL-----ERKAEL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 288 ENcdiklQAAELdnsslREEIARVREQLETARTDKAQLENDLREARREADA--ARESERHAISRANEAHHMLDVmreels 365
Cdd:COG1842    97 EA-----QAEAL-----EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTlkARAKAAKAQEKVNEALSGIDS------ 160

                         170       180
                  ....*....|....*....|....*...
gi 1009411338 366 lrNEDQQRLEELVQQVVQLQARNKSLEE 393
Cdd:COG1842   161 --DDATSALERMEEKIEEMEARAEAAAE 186
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
196-397 1.41e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 196 VYSDVSLEDVMDLSHKVQMIQEQMDALADTKSvgEERYTRAKQENATLharilmLEEAAKDAETRAEERLQAEQRRHREW 275
Cdd:COG4717   330 LPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAAL------LAEAGVEDEEELRAALEQAEEYQELK 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 276 ASRLERERQLQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAisranEAHH 355
Cdd:COG4717   402 EELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-----ELLQ 476

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1009411338 356 MLDVMREELSLRNEDQQRLeELVQQVVQlqarnKSLEESRDE 397
Cdd:COG4717   477 ELEELKAELRELAEEWAAL-KLALELLE-----EAREEYREE 512
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 211-364 1.42e-06

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 211 KVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAE---TRAEERLQAEQRRHREWASRL-----ERE 282
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKYEEQLgnvrnNKE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 283 RQ-LQLEncdikLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMR 361
Cdd:COG1579    91 YEaLQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165


                  ...
gi 1009411338 362 EEL 364
Cdd:COG1579   166 EEL 168
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 207-396 1.47e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.15  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 207 DLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHR----------EWA 276
Cdd:COG4942    52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspEDF 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 277 SRLERERQ-LQLENCDIKLQAAELDNSslREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAhh 355
Cdd:COG4942   132 LDAVRRLQyLKYLAPARREQAEELRAD--LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE-- 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1009411338 356 mLDVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRD 396
Cdd:COG4942   208 -LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 203-463 2.03e-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: 50.44  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRaEERLQAEQRRHREWASRLERE 282
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-LANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  283 RQLQLENcdikLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAAReserhaiSRANEAHHMLDVMRE 362
Cdd:TIGR02168  332 LDELAEE----LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-------SKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  363 ELSLRNEDQQRLEELVQQVVQ-LQARNKSLEESRDELQAAAALQAGRELIMLNPCNNNAEKGPSLAVELLAGMNPDQIDG 441
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480

                          250       260
                   ....*....|....*....|..
gi 1009411338  442 KGELSEPCTMAELKQALKEQQE 463
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQENLE 502
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
203-396 2.50e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEErLQAEQRRHREwasrlere 282
Cdd:PRK02224  328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-LEEEIEELRE-------- 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 283 rqlQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAAR--------ESERHAiSRANEAH 354
Cdd:PRK02224  399 ---RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHV-ETIEEDR 474

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1009411338 355 HMLDVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRD 396
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
294-397 8.49e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 8.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 294 LQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSLRNED--- 370
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEaee 112

                          90       100
                  ....*....|....*....|....*...
gi 1009411338 371 -QQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG4372   113 lQEELEELQKERQDLEQQRKQLEAQIAE 140
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-397 1.15e-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: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  230 EERYTRAKQENATLHARILMLEEAAKDAEtraEERLQAEQRRHREWASRLERERQLQLENCDIKLQAAELDN-----SSL 304
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDEL 808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  305 REEIARVREQLETARTDKAQLENDLREARREADAARES---ERHAISRANEAHHMLDVMREELslrnedQQRLEELVQQV 381
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieeLSEDIESLAAEIEELEELIEEL------ESELEALLNER 882

                          170
                   ....*....|....*.
gi 1009411338  382 VQLQARNKSLEESRDE 397
Cdd:TIGR02168  883 ASLEEALALLRSELEE 898
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
 251-380 1.26e-05

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 45.08  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 251 EEAAKDAETRAEERLQAEQRRHREWASRLERERQLQLENcDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLR 330
Cdd:pfam07321  12 EDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQE-EQRLYAEIQGKLVLLKELEKVKQQVALLRENEADLEKQVA 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1009411338 331 EARREADAARESERHAISRANEAHHMLDVMREELSLRNED----QQRLEELVQQ 380
Cdd:pfam07321  91 EARQQLEAEREALRQARQALAEARRAVEKFAELVRLVQAEelrqQERQEEQELE 144
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 230-411 1.57e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.43  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 230 EERYTRAKQENATLHARILMLEEA--AKDAETRAEERLQAEQRRhrewaSRLERERQL--------QLENCDIKLQAAEL 299
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAekARQAEMDRQAAIYAEQER-----MAMERERELerirqeerKRELERIRQEEIAM 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 300 DNSSLRE----------EIARVREQLETARTDKAQLEN----------DLREARREADAARESERHAISRaNEAHHMLDV 359
Cdd:pfam17380 373 EISRMRElerlqmerqqKNERVRQELEAARKVKILEEErqrkiqqqkvEMEQIRAEQEEARQREVRRLEE-ERAREMERV 451

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1009411338 360 MREELslrnEDQQRLEELVQQvvQLQARNKSLEESRDELQAAAALQAGRELI 411
Cdd:pfam17380 452 RLEEQ----ERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRAEEQRRKIL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-492 1.58e-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: 47.74  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  237 KQENATLHARILMLEEAAKDAET--------------------RAEERLQAEQRRHREWASRLERE-RQLQLENCDIKLQ 295
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKalaelrkeleeleeeleqlrKELEELSRQISALRKDLARLEAEvEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  296 AAELDN--SSLREEIARVREQLETARTDKAQLENDLREARREADAARE---SERHAISRANEAHHMLDVMREELSLRNED 370
Cdd:TIGR02168  756 LTELEAeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  371 -QQRLEELVQQVVQLQARNKSLEESRDELQAAAALQAgRELIMLNPCNNNAEKGPSLAVELLAGMNPDQIDGKGELSepc 449
Cdd:TIGR02168  836 tERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNERASLEEALALLRSELEELSEELRELESKRS--- 911

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1009411338  450 tmaELKQALKEQQEVNSQLRTYIDGILLNIVENYPQLLEVKQM 492
Cdd:TIGR02168  912 ---ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-413 1.81e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 216 QEQMDALADTksvgEERYTRAKQENATLHARILMLEEAAKDAETRAEeRLQAEQRRHREWASRLERERQLqlENCDIKLQ 295
Cdd:COG4717    77 EEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAEL--AELPERLE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 296 AAELDnsslREEIARVREQLETARTDKAQLENDLREARREADAAresERHAISRANEAHHMLDVMREELslrnedQQRLE 375
Cdd:COG4717   150 ELEER----LEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAEL------EEELE 216

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1009411338 376 ELVQQVVQLQARNKSLEESRDELQAAAALQAGRELIML 413
Cdd:COG4717   217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-397 3.42e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  202 LEDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARIlmleeaakdaeTRAEERLQAEQRRHREWASRLER 281
Cdd:COG4913    677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL-----------EQAEEELDELQDRLEAAEDLARL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  282 ERQLQLENcdiKLQAAELDNsSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMR 361
Cdd:COG4913    746 ELRALLEE---RFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALL 821

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1009411338  362 EElsLRNED----QQRLEELVQQ-----VVQLQARnksLEESRDE 397
Cdd:COG4913    822 DR--LEEDGlpeyEERFKELLNEnsiefVADLLSK---LRRAIRE 861
PTZ00121 PTZ00121
MAEBL; Provisional
 230-395 3.91e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 3.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  230 EERYTRAKQENATLHARIlmlEEA--AKDAETRAEERLQAEQRRHREWASRLERERQlqlencdiklqaAELDNsslREE 307
Cdd:PTZ00121  1094 EEAFGKAEEAKKTETGKA---EEArkAEEAKKKAEDARKAEEARKAEDARKAEEARK------------AEDAK---RVE 1155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  308 IARvreQLETARtdKAQLENDLREARReADAARESERhaISRANEAHHMLDVMREELSLRNEDQQRLEEL--------VQ 379
Cdd:PTZ00121  1156 IAR---KAEDAR--KAEEARKAEDAKK-AEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEArkaedakkAE 1227

                          170
                   ....*....|....*.
gi 1009411338  380 QVVQLQARNKSLEESR 395
Cdd:PTZ00121  1228 AVKKAEEAKKDAEEAK 1243
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 241-397 6.81e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 241 ATLHARILMLEEAAKDAEtraeERLQAEQRRHREWASRLERERQlQLENCDIKLQAAELDNSSLREEIARVREQLETART 320
Cdd:COG1579    13 QELDSELDRLEHRLKELP----AELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 321 DK--AQLENDLREARREADAARESERHAISRANEAHHMLDVMREELSLRNED-QQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG1579    88 NKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAELEAELEELEAEREE 167
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 231-397 1.29e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  231 ERYTRAKQENATLHARILMLEeaAKDAETRAEERLQAEQRrhrewASRLERERQLQLENCDIKLQAAELDNSSLREEIAR 310
Cdd:TIGR02168  213 ERYKELKAELRELELALLVLR--LEELREELEELQEELKE-----AEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  311 VREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREELslrNEDQQRLEELVQQVVQLQARNKS 390
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL---AELEEKLEELKEELESLEAELEE 362


                   ....*..
gi 1009411338  391 LEESRDE 397
Cdd:TIGR02168  363 LEAELEE 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-397 1.45e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  207 DLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERL-QAEQRRHREWASRLERER-Q 284
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEElE 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  285 LQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREEL 364
Cdd:TIGR02168  866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  365 S------------------------------LRN-----------------EDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:TIGR02168  946 SeeysltleeaealenkieddeeearrrlkrLENkikelgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
201-397 3.25e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 201 SLEDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEE-RLQAEqrRHREWASRL 279
Cdd:PRK02224  500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEaEEEAE--EAREEVAEL 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 280 ERERQLQLENCD----IKLQAAELDN-----SSLREEIARV-------REQLETARTDKAQLENDLREAR-READAARES 342
Cdd:PRK02224  578 NSKLAELKERIEslerIRTLLAAIADaedeiERLREKREALaelnderRERLAEKRERKRELEAEFDEARiEEAREDKER 657

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 343 ERHAISRANEAHHMLDVMREEL-----SLRNEdQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:PRK02224  658 AEEYLEQVEEKLDELREERDDLqaeigAVENE-LEELEELRERREALENRVEALEALYDE 716
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
231-397 3.32e-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: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 231 ERYTRAKQENATlhARILMLEEAAKDAETR---AEERLQAEQRRHRewASRLERERQL---QLENCDIKLQAAELDNSSL 304
Cdd:COG3206   163 EQNLELRREEAR--KALEFLEEQLPELRKEleeAEAALEEFRQKNG--LVDLSEEAKLllqQLSELESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 305 REEIARVREQLETARTDKAQLEND-----LREARREADAARESERhaiSRANEAHHMLDVMREEL-----SLRNEDQQRL 374
Cdd:COG3206   239 EARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELS---ARYTPNHPDVIALRAQIaalraQLQQEAQRIL 315

                         170       180
                  ....*....|....*....|...
gi 1009411338 375 EELVQQVVQLQARNKSLEESRDE 397
Cdd:COG3206   316 ASLEAELEALQAREASLQAQLAQ 338
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
251-396 3.96e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 251 EEAAKDAETRAEERLQAEQRRHREWASRLERerqlqlencdikLQAaelDNSSLREEIARVREQLEtartdkaQLENDLR 330
Cdd:COG2433   394 EPEAEREKEHEERELTEEEEEIRRLEEQVER------------LEA---EVEELEAELEEKDERIE-------RLERELS 451

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009411338 331 EARREADAARESERHAISRANEahhmLDVMREELslrNEDQQRLEELVQQVVQLQARNKsLEESRD 396
Cdd:COG2433   452 EARSEERREIRKDREISRLDRE----IERLEREL---EEERERIEELKRKLERLKELWK-LEHSGE 509
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 204-393 4.30e-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: 4.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  204 DVMDLSHKVQMIQEQMDALADTKSVGEERytrAKQENATLHARILMLEEAAkdAETRAEERlqaEQRRHREwaSRLER-E 282
Cdd:pfam15921  279 EITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV--SQLRSELR---EAKRMYE--DKIEElE 348

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  283 RQLQLENCDIKLQAAELDNSSlrEEIARVREQLEtartdkaQLENDLREARREADAARESERHAISRANEAHHMLDVMRE 362
Cdd:pfam15921  349 KQLVLANSELTEARTERDQFS--QESGNLDDQLQ-------KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR 419

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1009411338  363 ELSLRNEDQQRLEELV------------QQVVQLQARNKSLEE 393
Cdd:pfam15921  420 ELDDRNMEVQRLEALLkamksecqgqmeRQMAAIQGKNESLEK 462
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 203-397 6.89e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 6.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 203 EDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARIlmlEEAAKDAETrAEERLQAEQRRHREWAsrlere 282
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAE-AEAEIEERREELGERA------ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 283 RQLQLENCDIKLQAAELDNSSLREEIARVrEQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMRE 362
Cdd:COG3883    93 RALYRSGGSVSYLDVLLGSESFSDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1009411338 363 EL-SLRNEDQQRLEELVQQVVQLQARNKSLEESRDE 397
Cdd:COG3883   172 ELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 187-397 7.80e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 187 GSNYDATDDVYSDVSLEDVMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQ 266
Cdd:COG1196   600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 267 AEQRRHREwASRLERERQLQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHA 346
Cdd:COG1196   680 ELEELAER-LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009411338 347 ISRANEAHHMLDVMREELS------LR-----NEDQQRLEELVQQvvqlqarNKSLEESRDE 397
Cdd:COG1196   759 PPDLEELERELERLEREIEalgpvnLLaieeyEELEERYDFLSEQ-------REDLEEARET 813
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
283-410 9.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  283 RQLQLENCDIKLQAAELdnSSLREEIARVREQLETARTDKAQLEnDLREARREADAARESERH-----AISRANEAHHML 357
Cdd:COG4913    214 REYMLEEPDTFEAADAL--VEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAEleylrAALRLWFAQRRL 290

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1009411338  358 DVMREELSLRNEDQQRLEElvqQVVQLQARNKSLEESRDELQAAAALQAGREL 410
Cdd:COG4913    291 ELLEAELEELRAELARLEA---ELERLEARLDALREELDELEAQIRGNGGDRL 340
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
 257-350 9.79e-04

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 41.37  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 257 AETRAEERLQAEQRRHREWASRLERER---------QLQLENCDIKlqaaeldnsslreeiARVREQLETARTDKAQLEN 327
Cdd:PRK00247  288 AEQRAQYREKQKEKKAFLWTLRRNRLRmiitpwrapELHAENAEIK---------------KTRTAEKNEAKARKKEIAQ 352

                          90       100
                  ....*....|....*....|....
gi 1009411338 328 DLREARREADAARESER-HAISRA 350
Cdd:PRK00247  353 KRRAAEREINREARQERaAAMARA 376
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 215-395 1.40e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 41.32  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  215 IQEQMDALADTKSVGEERYTRAkQENATLHARIlmleeaaKDAETRAEERLQAEQRRHREWASRLERERQLQLENCDIKL 294
Cdd:PRK10246   299 IQEQSAALAHTRQQIEEVNTRL-QSTMALRARI-------RHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRA 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  295 QAAELDNSslREEIARVREQLETARTDKAQL-ENDLREARREADAAResERHAISRAneAHHMLDVMREELSLRNEDQQR 373
Cdd:PRK10246   371 QFSQQTSD--REQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAAL--AQHAEQRP--LRQRLVALHGQIVPQQKRLAQ 444

                          170       180
                   ....*....|....*....|...
gi 1009411338  374 LEELVQQVVQLQA-RNKSLEESR 395
Cdd:PRK10246   445 LQVAIQNVTQEQTqRNAALNEMR 467
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 201-393 1.48e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  201 SLEDvMDLSHKVQMIQEQMDALADTKSVGEERYTRAKQENATLHARilmleeaakdaETRAEERLQAEQRRHREWASRLE 280
Cdd:TIGR02169  783 DLEA-RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE-----------KEYLEKEIQELQEQRIDLKEQIK 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  281 RERQlQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARR---EADAARESERHAISRANEA---- 353
Cdd:TIGR02169  851 SIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKleal 929

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1009411338  354 ----HHMLDVMREELSLRNEDQQrLEELVQQVVQLQARNKSLEE 393
Cdd:TIGR02169  930 eeelSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEP 972
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
250-396 2.19e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 250 LEEAAKDAETRAEERLQAEQRRHrEWASRLERERQL-----QLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQ 324
Cdd:PRK02224  470 IEEDRERVEELEAELEDLEEEVE-EVEERLERAEDLveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009411338 325 LENdlrearrEADAARESERHAISRANEAHHMLDVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRD 396
Cdd:PRK02224  549 LEA-------EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 206-392 2.21e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 206 MDLSHKVQMIQEQMDALADTKSVGEER------------YTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHR 273
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERqrkiqqqkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 274 EWASRLERER-QLQLENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANE 352
Cdd:pfam17380 465 LRQQEEERKRkKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1009411338 353 AHHMLDVMR--EELSLRNEDQQRLE------ELVQQVVQLQARNKSLE 392
Cdd:pfam17380 545 QQEMEERRRiqEQMRKATEERSRLEamererEMMRQIVESEKARAEYE 592
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 206-418 2.83e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 206 MDLSHKVQMIQEqMDALADTKSVGEERYTRAKQENATLharilmLEEAaKDAETRAEERLQAEQRrhrewASRLERERQL 285
Cdd:pfam05483 384 MELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKL------LDEK-KQFEKIAEELKGKEQE-----LIFLLQAREK 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 286 QLENCDIKLQAAELDNSSLREEIARVREQLE---------TARTDKAQLENdlREARREA-DAARESERHA---ISRANE 352
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknielTAHCDKLLLEN--KELTQEAsDMTLELKKHQediINCKKQ 528

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 353 AHHML----DVMREELSLRNEDQQRLEELVQQVVQLQARNKSLEESRDELQAAAALQAGRELIMLNPCNN 418
Cdd:pfam05483 529 EERMLkqieNLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
PRK12472 PRK12472
hypothetical protein; Provisional
 241-353 3.14e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 39.85  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 241 ATLHARILMLEEAAKDAETRAEERLQAEQRRHREWAS------RLERER---QLQLENCDIKLQAAELDNSSLREEIAR- 310
Cdd:PRK12472  186 AAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPlkaslrKLERAKaraDAELKRADKALAAAKTDEAKARAEERQq 265

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1009411338 311 --------VREQLETARTDKAQLENDLREARREADAARESERHAISRANEA 353
Cdd:PRK12472  266 kaaqqaaeAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDA 316
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 211-397 3.73e-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: 40.21  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  211 KVQMIQEQMDALadtksvgEERYTRAKQENA-TLHARILMLEEAAKDAETrAEERLQAEQRRHREWASRLERERQLQLEN 289
Cdd:pfam12128  316 AVAKDRSELEAL-------EDQHGAFLDADIeTAAADQEQLPSWQSELEN-LEERLKALTGKHQDVTAKYNRRRSKIKEQ 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  290 CDIKLQAAELDNSSLREEIARvreQLETARTDKAQLENDLREARREAdaareserhaISRANEAHHMLDVMREELSLRNE 369
Cdd:pfam12128  388 NNRDIAGIKDKLAKIREARDR---QLAVAEDDLQALESELREQLEAG----------KLEFNEEEYRLKSRLGELKLRLN 454

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1009411338  370 DQQRLEELVQQVVQ-----------LQARNKSLEESRDE 397
Cdd:pfam12128  455 QATATPELLLQLENfderierareeQEAANAEVERLQSE 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-397 3.80e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  230 EERYTRAKQENATLHARI----LMLEEAAKDAETRAEERLQAEqrRHREWASRLER----ERQLQLENCDIKLQAAELDN 301
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIerldLIIDEKRQQLERLRREREKAE--RYQALLKEKREyegyELLKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  302 SSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRaneahHMLDVMREELSLRN---EDQQRLEELV 378
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-----KIGELEAEIASLERsiaEKERELEDAE 321

                          170
                   ....*....|....*....
gi 1009411338  379 QQVVQLQARNKSLEESRDE 397
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEE 340
PTZ00121 PTZ00121
MAEBL; Provisional
 251-395 5.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  251 EEAAKDAETRAEERLQAEQRRHREWASRLERERQLQLENC----DIKLQAAELDNS-----------SLREEIARVREQL 315
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAeeekkkveqlkKKEAEEKKKAEEL 1652

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  316 ----ETARTDKAQLENDLREARREADAARESER------HAISRANEAHHMLDVMR--EELSLRNEDQQRLEELVQQVVQ 383
Cdd:PTZ00121  1653 kkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkaaEALKKEAEEAKKAEELKkkEAEEKKKAEELKKAEEENKIKA 1732

                          170
                   ....*....|..
gi 1009411338  384 LQARNKSLEESR 395
Cdd:PTZ00121  1733 EEAKKEAEEDKK 1744
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-397 5.84e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  276 ASRLERERQLqlENCDIKLQAAELDNSSLREEIARVREQLETARTDKAQLENDLREARREADAAR--------ESERHAI 347
Cdd:TIGR02168  670 SSILERRREI--EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlarleaEVEQLEE 747

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009411338  348 SRAN-------------EAHHMLDVMREELSLRNEDQQRLEELVQqvvQLQARNKSLEESRDE 397
Cdd:TIGR02168  748 RIAQlskelteleaeieELEERLEEAEEELAEAEAEIEELEAQIE---QLKEELKALREALDE 807
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 294-384 5.87e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 294 LQAAELDNSSLREEIARVREQLETARTDKAQLendLREARREADAARESerhAISRAN-EAHHMLDVMREElsLRNEDQQ 372
Cdd:cd06503    39 LEEAEKAKEEAEELLAEYEEKLAEARAEAQEI---IEEARKEAEKIKEE---ILAEAKeEAERILEQAKAE--IEQEKEK 110

                          90
                  ....*....|..
gi 1009411338 373 RLEELVQQVVQL 384
Cdd:cd06503   111 ALAELRKEVADL 122
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 217-353 6.28e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 217 EQMDA-LADTKSVGEErYTRAKQENATLHARilmLEEAAKDAETRAEErLQAEQRRHREWASRLERERQLQLEncdIKLQ 295
Cdd:PRK09510   48 SVIDAvMVDPGAVVEQ-YNRQQQQQKSAKRA---EEQRKKKEQQQAEE-LQQKQAAEQERLKQLEKERLAAQE---QKKQ 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1009411338 296 AAELDNSSLREEIARVREQLETARTDKAQLEndlREARREADAARESERHAISRANEA 353
Cdd:PRK09510  120 AEEAAKQAALKQKQAEEAAAKAAAAAKAKAE---AEAKRAAAAAKKAAAEAKKKAEAE 174
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 302-397 6.30e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.85  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 302 SSLREEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRANEAHHMLDVMREEL-SLRNEDQQRLEELVQQ 380
Cdd:pfam07926   4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQALREELnELKAEIAELKAEAESA 83

                          90
                  ....*....|....*..
gi 1009411338 381 VVQLQARNKSLEESRDE 397
Cdd:pfam07926  84 KAELEESEESWEEQKKE 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
305-397 6.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  305 REEIARVREQLETARTDKAQLENDLREARREADAARESERHAISRAN---------EAHHMLDVMREELSLRNEDQQRLE 375
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELERLDASSDDLA 688

                           90       100
                   ....*....|....*....|..
gi 1009411338  376 ELVQQVVQLQARNKSLEESRDE 397
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDE 710
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-396 8.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 216 QEQMDALADTKSVGEERYTRAKQENATLHARILMLEEAAKDAETRAEERLQAEQRRHREWAsrlERERQLQLENCDIKLQ 295
Cdd:COG4717   297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---ELEEELQLEELEQEIA 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 296 A-AELDNSSLREEIARVREQLETARtdkaQLENDLREARREADAARESERHAISRANEA--HHMLDVMREELslrNEDQQ 372
Cdd:COG4717   374 AlLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEEL---EELEE 446

                         170       180
                  ....*....|....*....|....
gi 1009411338 373 RLEELVQQVVQLQARNKSLEESRD 396
Cdd:COG4717   447 ELEELREELAELEAELEQLEEDGE 470
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
230-341 8.42e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 230 EERYTRAKQENATLHARILmlEEAAKDAETRAEERLQAEQ-RRHREWASRLERERQLQLENCDIKLQAAELDNSSLREEI 308
Cdd:COG2268   222 EAEEAELEQEREIETARIA--EAEAELAKKKAEERREAETaRAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1009411338 309 ARVREQLETARTDKAQLE--NDLREARREADAARE 341
Cdd:COG2268   300 EREEAELEADVRKPAEAEkqAAEAEAEAEAEAIRA 334
PTZ00121 PTZ00121
MAEBL; Provisional
 182-377 8.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  182 NSSGMGSNYDATDDVYSDVSLEDVMDLSHKVQmiqEQMDALADTKSVGEERYTRAKQENATLHAR----ILMLEEAAKDA 257
Cdd:PTZ00121  1073 KPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---KTETGKAEEARKAEEAKKKAEDARKAEEARkaedARKAEEARKAE 1149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338  258 ETR-------AEERLQAEQRRHREWASRLERERQLQLENCDIKLQAAE----LDNSSLREEIARVREQLETARTDKAQLE 326
Cdd:PTZ00121  1150 DAKrveiarkAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarkAEAARKAEEERKAEEARKAEDAKKAEAV 1229

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1009411338  327 NDLREARREADAARESER---HAISRANEAHHMLDVMREELSLRNEDQQRLEEL 377
Cdd:PTZ00121  1230 KKAEEAKKDAEEAKKAEEernNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 253-353 9.82e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 38.39  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009411338 253 AAKdAE--TRAEERLQAEQRRHREWA--SRLERERQLQLEncdiKLQAA-----ELDNSSLREEIARVREQ---LETART 320
Cdd:PRK05035  433 QAK-AEirAIEQEKKKAEEAKARFEArqARLEREKAAREA----RHKKAaearaAKDKDAVAAALARVKAKkaaATQPIV 507

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1009411338 321 DKAQLENDLREARREADAARESERHAISRANEA 353
Cdd:PRK05035  508 IKAGARPDNSAVIAAREARKAQARARQAEKQAA 540
 
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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