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Conserved domains on  [gi|568975824|ref|XP_006534281|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform X10 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40_2 super family cl41045
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 801-1019 6.01e-41

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


The actual alignment was detected with superfamily member pfam19056:

Pssm-ID: 465964  Cd Length: 487  Bit Score: 158.26  E-value: 6.01e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   801 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 878
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   879 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 958
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975824   959 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1019
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 253-321 9.30e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


:

Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.01  E-value: 9.30e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824   253 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 321
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 296-489 2.69e-05

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.58  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 375
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   376 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 453
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975824   454 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 489
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-333 1.06e-03

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   226 fEELSSAGSGLIGDVDEGADLLGEYSGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 304
Cdd:TIGR04523  499 -KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 568975824   305 AKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 801-1019 6.01e-41

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 158.26  E-value: 6.01e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   801 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 878
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   879 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 958
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975824   959 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1019
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 253-321 9.30e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.01  E-value: 9.30e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824   253 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 321
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 296-489 2.69e-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: 48.58  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 375
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   376 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 453
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975824   454 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 489
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
256-399 1.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  256 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 321
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824  322 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 399
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-380 1.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  266 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 345
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975824  346 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 380
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
818-1015 2.42e-04

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  818 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 890
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  891 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 963
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975824  964 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1015
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-375 2.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  249 EYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAE 328
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568975824  329 DARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 375
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-374 3.41e-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: 45.05  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   163 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAgSGLIGDV 240
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANL 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   241 DEG-ADLLGEYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE 319
Cdd:TIGR02168  823 RERlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568975824   320 LRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 374
Cdd:TIGR02168  903 LRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 245-377 8.12e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 42.34  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  245 DLLGEYSGMGREVENLILENTQLLETknaLNVVKNDLIAKvdeltcekdvlQGELEAVKQAKLKLEDKNRELEEELRKAR 324
Cdd:cd07596    93 EPLKEYLRYCQAVKETLDDRADALLT---LQSLKKDLASK-----------KAQLEKLKAAPGIKPAKVEELEEELEEAE 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  325 AEAEDARQKAkdDDDSDIPTAQRKRFTR---VEMARVLME--RNQ--YKERLMELQEAVR 377
Cdd:cd07596   159 SALEEARKRY--EEISERLKEELKRFHEeraRDLKAALKEfaRLQvqYAEKIAEAWESLL 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 255-377 9.09e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   255 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 325
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975824   326 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 377
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-333 1.06e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   226 fEELSSAGSGLIGDVDEGADLLGEYSGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 304
Cdd:TIGR04523  499 -KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 568975824   305 AKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-384 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  153 KSEISKHIEvqvAQETRNVSTESGENEEKSEVQAIIESTPELdmdKDLSGYKGSSTPTKGIENKAFD--RNTESLFEELS 230
Cdd:PRK03918  247 LESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKEL---KELKEKAEEYIKLSEFYEEYLDelREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  231 SAGSGLIGDVDEGAD-------LLGEYSGMGREVENLiLENTQLLETKNALNVVKNDLIAKVDELTCEKdvLQGELEAVK 303
Cdd:PRK03918  321 EEINGIEERIKELEEkeerleeLKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  304 QAKLKLEDKNRELEEELRKARAEAEDAR------QKAKddddSDIPTAQR-----------KRFTRvEMARVLMERNQYK 366
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELKkaieelKKAK----GKCPVCGRelteehrkellEEYTA-ELKRIEKELKEIE 472

                         250
                  ....*....|....*...
gi 568975824  367 ERLMELQEAVRWTEMIRA 384
Cdd:PRK03918  473 EKERKLRKELRELEKVLK 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-534 2.03e-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: 42.35  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   264 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 342
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   343 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 416
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   417 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 493
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568975824   494 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 534
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-401 2.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  176 GENEE-KSEVQAIIESTPELDMDKDLSG-YKGSstptkGIENKAFDRNTESLFEELSSAGSgligDVDEGADLLGEYSGM 253
Cdd:COG4717    30 GPNEAgKSTLLAFIRAMLLERLEKEADElFKPQ-----GRKPELNLKELKELEEELKEAEE----KEEEYAELQEELEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  254 GREVENL----------------ILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 317
Cdd:COG4717   101 EEELEELeaeleelreeleklekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  318 EELRKARAEAEDARQKAKDdddsdiptaqrkrftrvEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRS 397
Cdd:COG4717   181 ELLEQLSLATEEELQDLAE-----------------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                  ....
gi 568975824  398 SIWQ 401
Cdd:COG4717   244 RLKE 247
growth_prot_Scy NF041483
polarized growth protein Scy;
310-397 2.33e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  310 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 384
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975824  385 SRENPAMQEKKRS 397
Cdd:NF041483  344 EKLVAEAAEKART 356
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 253-382 3.58e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 40.12  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  253 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 332
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975824  333 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 382
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 801-1019 6.01e-41

WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.


Pssm-ID: 465964  Cd Length: 487  Bit Score: 158.26  E-value: 6.01e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   801 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 878
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   879 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 958
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975824   959 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1019
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 253-321 9.30e-28

JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of several JNK-interacting proteins (JIP). It interacts with the small GTP-binding protein ARF6.


Pssm-ID: 465127 [Multi-domain]  Cd Length: 69  Bit Score: 107.01  E-value: 9.30e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824   253 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 321
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 296-489 2.69e-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: 48.58  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 375
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   376 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 453
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975824   454 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 489
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 278-387 6.04e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 43.75  E-value: 6.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   278 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE---LRKARAEAEDARQKAKDdddsdipTAQRKRFTRVE 354
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEE-------SAEMEAEEKEQ 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568975824   355 MARVLMERNQYKERLMEL-----QEAVRW-TEMIRASRE 387
Cdd:pfam20492   81 LEAELAEAQEEIARLEEEverkeEEARRLqEELEEAREE 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
256-399 1.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  256 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 321
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824  322 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 399
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
266-380 1.77e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  266 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 345
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975824  346 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 380
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
818-1015 2.42e-04

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  818 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 890
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  891 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 963
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975824  964 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1015
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-375 2.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  249 EYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAE 328
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568975824  329 DARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 375
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 298-396 3.19e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   298 ELEAVKQA-KLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLmernqykERLMELQEAV 376
Cdd:pfam13868  233 QRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL-------EKQIEEREEQ 305

                           90       100
                   ....*....|....*....|
gi 568975824   377 RWTEMIRASRENPAMQEKKR 396
Cdd:pfam13868  306 RAAEREEELEEGERLREEEA 325
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-374 3.41e-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: 45.05  E-value: 3.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   163 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAgSGLIGDV 240
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANL 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   241 DEG-ADLLGEYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE 319
Cdd:TIGR02168  823 RERlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568975824   320 LRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 374
Cdd:TIGR02168  903 LRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 300-396 4.02e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   300 EAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKddddsdiptaqrkrftrvEMArvlMERNQYKERLMEL-QEAVRW 378
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE------------------ELE---EERRQAEEEAERLeQKRQEA 60

                           90
                   ....*....|....*...
gi 568975824   379 TEMIRASRENPAMQEKKR 396
Cdd:pfam20492   61 EEEKERLEESAEMEAEEK 78
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 296-337 4.26e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 42.08  E-value: 4.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975824  296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 337
Cdd:COG0711    37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 255-396 7.60e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 7.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  255 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 334
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975824  335 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 396
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
279-387 7.83e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  279 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdipTAQRKRFTRVEMARV 358
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-------LQEEAEELQEELEEL 120

                          90       100
                  ....*....|....*....|....*....
gi 568975824  359 LMERNQYKERLMELQEAVRWTEMIRASRE 387
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAERE 149
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 245-377 8.12e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 42.34  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  245 DLLGEYSGMGREVENLILENTQLLETknaLNVVKNDLIAKvdeltcekdvlQGELEAVKQAKLKLEDKNRELEEELRKAR 324
Cdd:cd07596    93 EPLKEYLRYCQAVKETLDDRADALLT---LQSLKKDLASK-----------KAQLEKLKAAPGIKPAKVEELEEELEEAE 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  325 AEAEDARQKAkdDDDSDIPTAQRKRFTR---VEMARVLME--RNQ--YKERLMELQEAVR 377
Cdd:cd07596   159 SALEEARKRY--EEISERLKEELKRFHEeraRDLKAALKEfaRLQvqYAEKIAEAWESLL 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 255-377 9.09e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 9.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   255 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 325
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975824   326 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 377
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
223-333 9.43e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 9.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  223 ESLFEELSSagsgLIGDVDEGADLLGEYSGMGREVENL---I--LENTQllETKNALNVVKNDLIAKVDELtcEKdvlqg 297
Cdd:COG1340    81 DELNEKLNE----LREELDELRKELAELNKAGGSIDKLrkeIerLEWRQ--QTEVLSPEEEKELVEKIKEL--EK----- 147

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975824  298 ELEAVKQAkLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:COG1340   148 ELEKAKKA-LEKNEKLKELRAELKELRKEAEEIHKK 182
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-333 1.06e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   226 fEELSSAGSGLIGDVDEGADLLGEYSGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 304
Cdd:TIGR04523  499 -KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 568975824   305 AKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 269-376 1.10e-03

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 40.07  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   269 ETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKlKLEDKNRELEEELRKARAEAEDARQKAKDDDdsdiptaqrk 348
Cdd:pfam04871    5 ELESEASSLKNENTELKAELQELSKQYNSLEQKESQAK-ELEAEVKKLEEALKKLKAELSEEKQKEKEKQ---------- 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568975824   349 rfTRVEMARVLM-----ERNQYKERLMELQEAV 376
Cdd:pfam04871   74 --SELDDLLLLLgdleeKVEKYKARLKELGEEV 104
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-384 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  153 KSEISKHIEvqvAQETRNVSTESGENEEKSEVQAIIESTPELdmdKDLSGYKGSSTPTKGIENKAFD--RNTESLFEELS 230
Cdd:PRK03918  247 LESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKEL---KELKEKAEEYIKLSEFYEEYLDelREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  231 SAGSGLIGDVDEGAD-------LLGEYSGMGREVENLiLENTQLLETKNALNVVKNDLIAKVDELTCEKdvLQGELEAVK 303
Cdd:PRK03918  321 EEINGIEERIKELEEkeerleeLKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  304 QAKLKLEDKNRELEEELRKARAEAEDAR------QKAKddddSDIPTAQR-----------KRFTRvEMARVLMERNQYK 366
Cdd:PRK03918  398 KAKEEIEEEISKITARIGELKKEIKELKkaieelKKAK----GKCPVCGRelteehrkellEEYTA-ELKRIEKELKEIE 472

                         250
                  ....*....|....*...
gi 568975824  367 ERLMELQEAVRWTEMIRA 384
Cdd:PRK03918  473 EKERKLRKELRELEKVLK 490
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 296-337 1.32e-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: 40.11  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975824  296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 337
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 255-391 1.69e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  255 REVENLILENTQLLET-KNALNVVKNdliakVDELtcekDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:COG1579    62 KRLELEIEEVEARIKKyEEQLGNVRN-----NKEY----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975824  334 AKD-DDDSDIPTAQRKRF---TRVEMARVLMERNQYKERLMElqEAVRWTEMIRASRENPAM 391
Cdd:COG1579   133 LAElEAELEEKKAELDEElaeLEAELEELEAEREELAAKIPP--ELLALYERIRKRKNGLAV 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 255-396 1.72e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   255 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQaklKLEDKNRELEEeLRKARAEAE---DAR 331
Cdd:pfam13868  145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE---KAQDEKAERDE-LRAKLYQEEqerKER 220

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975824   332 QKAKDDddsdiptAQRKRFTRVEMARVLMERNQYKERL--MELQEAVRWTEMIRAS----RENPAMQEKKR 396
Cdd:pfam13868  221 QKEREE-------AEKKARQRQELQQAREEQIELKERRlaEEAEREEEEFERMLRKqaedEEIEQEEAEKR 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-534 2.03e-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: 42.35  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   264 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 342
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   343 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 416
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   417 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 493
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568975824   494 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 534
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 291-375 2.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  291 EKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDipTAQRKRFTRV--EMARVLMERNQYKER 368
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELlaELARLEQDIARLEER 310


                  ....*..
gi 568975824  369 LMELQEA 375
Cdd:COG1196   311 RRELEER 317
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
176-401 2.32e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  176 GENEE-KSEVQAIIESTPELDMDKDLSG-YKGSstptkGIENKAFDRNTESLFEELSSAGSgligDVDEGADLLGEYSGM 253
Cdd:COG4717    30 GPNEAgKSTLLAFIRAMLLERLEKEADElFKPQ-----GRKPELNLKELKELEEELKEAEE----KEEEYAELQEELEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  254 GREVENL----------------ILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 317
Cdd:COG4717   101 EEELEELeaeleelreeleklekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  318 EELRKARAEAEDARQKAKDdddsdiptaqrkrftrvEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRS 397
Cdd:COG4717   181 ELLEQLSLATEEELQDLAE-----------------ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243


                  ....
gi 568975824  398 SIWQ 401
Cdd:COG4717   244 RLKE 247
growth_prot_Scy NF041483
polarized growth protein Scy;
310-397 2.33e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  310 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 384
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975824  385 SRENPAMQEKKRS 397
Cdd:NF041483  344 EKLVAEAAEKART 356
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 216-387 2.34e-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: 42.36  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   216 KAFDRNTESLFEELSSAGSgligDVDEGADLLGEYSGMGREVENlilENTQLLETKNALNvvkndliAKVDELTCEKDVL 295
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIEN----RLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLK-------ERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQkakDDDDSDIPTAQRK---------------RFTRVEMARVLM 360
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAElskleeevsriearlREIEQKLNRLTL 826

                          170       180
                   ....*....|....*....|....*..
gi 568975824   361 ERNQYKERLMELQEAVRWTEMIRASRE 387
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLKEQIKSIE 853
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 241-387 2.39e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  241 DEGADLLGEYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEEL 320
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975824  321 RKARAEAEDARQKAKDDDDSdipTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRwtEMIRASRE 387
Cdd:COG1196   361 AEAEEALLEAEAELAEAEEE---LEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEE 422
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-398 2.64e-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: 41.97  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   223 ESLFEELSSAGSGLIGDVDEGADLLGEYSGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDV-------L 295
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeieeL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAK-------DDDDSDIPTAQRKRFTRVEMARVLMERNQYKER 368
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568975824   369 LMELQEAV-RWTEMIRASRENPAMQEKKRSS 398
Cdd:TIGR02168  868 IEELESELeALLNERASLEEALALLRSELEE 898
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 281-375 3.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  281 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLM 360
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                          90
                  ....*....|....*
gi 568975824  361 ERNQYKERLMELQEA 375
Cdd:COG1196   324 ELAELEEELEELEEE 338
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 269-333 3.15e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568975824  269 ETKNALNVVKNDLIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:COG4026   132 ELREELLELKEKIDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 256-401 3.20e-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: 41.98  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   256 EVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAV-----------KQAKLKLEDKNRELEEELRKAR 324
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrdelKDYREKLEKLKREINELKRELD 409

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975824   325 AEAEDARQKakddddsdiptAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASRENPAMQEKKRSSIWQ 401
Cdd:TIGR02169  410 RLQEELQRL-----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE--WKLEQLAADLSKYEQELYD 473
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 253-382 3.58e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 40.12  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  253 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 332
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975824  333 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 382
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 264-380 4.42e-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: 41.20  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   264 NTQLLETKNALNVVK---NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKD---- 336
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnne 401

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568975824   337 ---------------DDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTE 380
Cdd:TIGR02168  402 ierlearlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
 266-362 5.97e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 40.76  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   266 QLLETKNALNVVKNDLIAKVDELtceKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 345
Cdd:pfam09798    5 KLELLQQEKEKELEKLKNSYEEL---KSSHEEELEKLKQEVQKLEDEKKFLLNELRSLSATSPASSQSHETDTDDSSSVS 81

                           90
                   ....*....|....*..
gi 568975824   346 QRKRFTRVEMARVLMER 362
Cdd:pfam09798   82 LKKRKIEESTAESLKQK 98
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 296-393 6.10e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   296 QGELEAVKQAKLKLEDKNRELEEE--LRKARAEAEDARQKAKddddsdiptaQRKRFTRVEMARVLMERNQ--YKERLME 371
Cdd:pfam15709  365 QEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEE----------ERKQRLQLQAAQERARQQQeeFRRKLQE 434

                           90       100
                   ....*....|....*....|..
gi 568975824   372 LQEAVRWTEMIRASRENPAMQE 393
Cdd:pfam15709  435 LQRKKQQEEAERAEAEKQRQKE 456
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 278-387 6.57e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824   278 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAED------ARQKAKDDDDSDIPTAQR--KR 349
Cdd:pfam01576  259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKREQEVTELKKalEE 338

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568975824   350 FTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 387
Cdd:pfam01576  339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE 376
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 271-333 8.46e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 8.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975824  271 KNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 281-333 9.60e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.09  E-value: 9.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568975824   281 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 333
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQER 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 279-421 9.88e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975824  279 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDArQKAKDDDDSDIPTAQRKrftrveMARV 358
Cdd:COG3883   115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-EAAKAELEAQQAEQEAL------LAQL 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975824  359 LMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATKKPEPPV 421
Cdd:COG3883   188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
 
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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