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Conserved domains on  [gi|312836825|ref|NP_001186134|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform 7 [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.
 797-1015 5.98e-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: 5.98e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   797 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 874
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   875 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 954
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836825   955 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1015
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 249-317 1.00e-27

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: 1.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   249 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 317
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 292-485 2.68e-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: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 371
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   372 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 449
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 312836825   450 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 485
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 ...
 151-329 5.59e-04

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: 44.24  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   226 fEELSSAGSGLIGDV----DEGADLLGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 300
Cdd:TIGR04523  499 -KKLNEEKKELEEKVkdltKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 312836825   301 AKLKLEDKNRELEEELRKARAEAEDARQK 329
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.
 797-1015 5.98e-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: 5.98e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   797 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 874
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   875 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 954
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836825   955 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1015
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 249-317 1.00e-27

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: 1.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   249 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 317
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 292-485 2.68e-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: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 371
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   372 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 449
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 312836825   450 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 485
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
252-395 1.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  252 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 317
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825  318 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 395
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-376 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 312836825  262 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 341
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312836825  342 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 376
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
814-1011 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 312836825  814 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 886
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  887 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 959
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836825  960 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1011
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 241-371 3.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  241 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 320
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312836825  321 AEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 371
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-370 3.85e-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: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   163 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELS-------SAG 233
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   234 SGLIGDVDEGADLLGMGREVENLILENTQLLEtknALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 313
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   314 EELRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 370
Cdd:TIGR02168  901 EELRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-329 5.59e-04

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: 44.24  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   226 fEELSSAGSGLIGDV----DEGADLLGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 300
Cdd:TIGR04523  499 -KKLNEEKKELEEKVkdltKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 312836825   301 AKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-373 9.21e-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: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   251 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 321
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 312836825   322 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 373
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 292-333 1.40e-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: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836825  292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 333
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-530 2.08e-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: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   260 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 338
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   339 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 412
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   413 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 489
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 312836825   490 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 530
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
growth_prot_Scy NF041483
polarized growth protein Scy;
306-393 2.32e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  306 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 380
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 312836825  381 SRENPAMQEKKRS 393
Cdd:NF041483  344 EKLVAEAAEKART 356
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 249-378 3.53e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 40.12  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  249 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 328
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836825  329 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 378
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 92-337 6.51e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   92 QELSQPRSHTSLKDEL---------SDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFvkgTDTSNKSEISKHIEV 162
Cdd:PLN03229  522 KRLSRAPNYLSLKYKLdmlnefsraKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEAL---KAEVASSGASSGDEL 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  163 QvaQETRNvSTESGENEEKSEVQAIIEStpeldMDKDLSGYKGSSTPT-KGIENKAFDRNTESLFEELSSAgsglIGDVD 241
Cdd:PLN03229  599 D--DDLKE-KVEKMKKEIELELAGVLKS-----MGLEVIGVTKKNKDTaEQTPPPNLQEKIESLNEEINKK----IERVI 666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  242 EGADLLGMgreVENLILENTQLLETKNAlnvvknDLIAKVDELtcEKDVLQGELEAVKQAKLKleDKNRELEEELRKAR- 320
Cdd:PLN03229  667 RSSDLKSK---IELLKLEVAKASKTPDV------TEKEKIEAL--EQQIKQKIAEALNSSELK--EKFEELEAELAAARe 733

                         250
                  ....*....|....*...
gi 312836825  321 -AEAEDARQKAKDDDDSD 337
Cdd:PLN03229  734 tAAESNGSLKNDDDKEED 751
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 159-276 7.83e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.79  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   159 HIEVQVAQ-ETRNVSTESGENEEKSEVQAIIESTPELDMDKD-LSGYKGSSTPTKGIENKAfDRNTESLFEELSS---AG 233
Cdd:pfam15905  195 HSKGKVAQlEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEqVEKYKLDIAQLEELLKEK-NDEIESLKQSLEEkeqEL 273

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 312836825   234 SGLIGDVDEGADLLgmGREVENLILE--------NTQLLETKNALNVVKND 276
Cdd:pfam15905  274 SKQIKDLNEKCKLL--ESEKEELLREyeekeqtlNAELEELKEKLTLEEQE 322
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 797-1015 5.98e-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: 5.98e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   797 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 874
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   875 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 954
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836825   955 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1015
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 249-317 1.00e-27

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: 1.00e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   249 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 317
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 292-485 2.68e-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: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 371
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   372 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 449
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 312836825   450 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 485
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 274-383 6.02e-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: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   274 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE---LRKARAEAEDARQKAKDdddsdipTAQRKRFTRVE 350
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEE-------SAEMEAEEKEQ 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 312836825   351 MARVLMERNQYKERLMEL-----QEAVRW-TEMIRASRE 383
Cdd:pfam20492   81 LEAELAEAQEEIARLEEEverkeEEARRLqEELEEAREE 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
252-395 1.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  252 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 317
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825  318 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 395
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-376 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 312836825  262 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 341
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 312836825  342 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 376
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
814-1011 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 312836825  814 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 886
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  887 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 959
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836825  960 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1011
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 241-371 3.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  241 DEGADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKAR 320
Cdd:COG1196   278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 312836825  321 AEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 371
Cdd:COG1196   358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 294-392 3.17e-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: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   294 ELEAVKQA-KLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLmernqykERLMELQEAV 372
Cdd:pfam13868  233 QRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL-------EKQIEEREEQ 305

                           90       100
                   ....*....|....*....|
gi 312836825   373 RWTEMIRASRENPAMQEKKR 392
Cdd:pfam13868  306 RAAEREEELEEGERLREEEA 325
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-370 3.85e-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: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   163 QVAQETRNVSTESGENEEKSEVQA--IIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELS-------SAG 233
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEerLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLR 823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   234 SGLIGDVDEGADLLGMGREVENLILENTQLLEtknALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELE 313
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   314 EELRKARAEAEDARQKAKddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 370
Cdd:TIGR02168  901 EELRELESKRSELRRELE---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 296-392 3.96e-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: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   296 EAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKddddsdiptaqrkrftrvEMArvlMERNQYKERLMEL-QEAVRW 374
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE------------------ELE---EERRQAEEEAERLeQKRQEA 60

                           90
                   ....*....|....*...
gi 312836825   375 TEMIRASRENPAMQEKKR 392
Cdd:pfam20492   61 EEEKERLEESAEMEAEEK 78
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 292-333 4.41e-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: 4.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836825  292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 333
Cdd:COG0711    37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 151-329 5.59e-04

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: 44.24  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   151 SNKSEISKHIEVQVAQETRNVSTESGENEEKSEVQAIIESTPEL--DMDKDLSGYKGSSTPTKG---IENKAFDRNTESL 225
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSRSINKIKQnleQKQKELKSKEKEL 498

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   226 fEELSSAGSGLIGDV----DEGADLLGMGREVENLILE-NTQLLETKNALNVVKNDLiaKVDELTCEKDVLQGELEAVKQ 300
Cdd:TIGR04523  499 -KKLNEEKKELEEKVkdltKKISSLKEKIEKLESEKKEkESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQ 575

                          170       180
                   ....*....|....*....|....*....
gi 312836825   301 AKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 251-392 7.57e-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: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  251 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 330
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312836825  331 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 392
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
275-383 8.00e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  275 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdipTAQRKRFTRVEMARV 354
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-------LQEEAEELQEELEEL 120

                          90       100
                  ....*....|....*....|....*....
gi 312836825  355 LMERNQYKERLMELQEAVRWTEMIRASRE 383
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-373 9.21e-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: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   251 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 321
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 312836825   322 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 373
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 265-372 1.09e-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: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   265 ETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKlKLEDKNRELEEELRKARAEAEDARQKAK----DDDDsdipt 340
Cdd:pfam04871    5 ELESEASSLKNENTELKAELQELSKQYNSLEQKESQAK-ELEAEVKKLEEALKKLKAELSEEKQKEKekqsELDD----- 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 312836825   341 aqrkrfTRVEMARVLMERNQYKERLMELQEAV 372
Cdd:pfam04871   79 ------LLLLLGDLEEKVEKYKARLKELGEEV 104
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 292-333 1.40e-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: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 312836825  292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 333
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 251-387 1.70e-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: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  251 REVENLILENTQLLET-KNALNVVKNdliakVDELtcekDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:COG1579    62 KRLELEIEEVEARIKKyEEQLGNVRN-----NKEY----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312836825  330 AKD-DDDSDIPTAQRKRF---TRVEMARVLMERNQYKERLMElqEAVRWTEMIRASRENPAM 387
Cdd:COG1579   133 LAElEAELEEKKAELDEElaeLEAELEELEAEREELAAKIPP--ELLALYERIRKRKNGLAV 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 251-392 1.73e-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: 41.83  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   251 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQaklKLEDKNRELEEeLRKARAEAE---DAR 327
Cdd:pfam13868  145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE---KAQDEKAERDE-LRAKLYQEEqerKER 220

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836825   328 QKAKDDddsdiptAQRKRFTRVEMARVLMERNQYKERL--MELQEAVRWTEMIRAS----RENPAMQEKKR 392
Cdd:pfam13868  221 QKEREE-------AEKKARQRQELQQAREEQIELKERRlaEEAEREEEEFERMLRKqaedEEIEQEEAEKR 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-530 2.08e-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: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   260 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 338
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   339 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 412
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   413 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 489
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 312836825   490 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 530
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 287-371 2.20e-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: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  287 EKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDipTAQRKRFTRV--EMARVLMERNQYKER 364
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELlaELARLEQDIARLEER 310


                  ....*..
gi 312836825  365 LMELQEA 371
Cdd:COG1196   311 RRELEER 317
growth_prot_Scy NF041483
polarized growth protein Scy;
306-393 2.32e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  306 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 380
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 312836825  381 SRENPAMQEKKRS 393
Cdd:NF041483  344 EKLVAEAAEKART 356
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
223-383 2.39e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  223 ESLFEELSSAGSGLIGDVDEGADLLGMGREVENLiLENTQLLEtknalnvvknDLIAKVDElTCEKDVLQgeLEAVKQAK 302
Cdd:PRK02224  481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLE----------ELIAERRE-TIEEKRER--AEELRERA 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  303 LKLEDKNRELEEELRKARAEAEDARQKAKD-DDDSDIPTAQRKRFTRVEmaRVLMERNQYKERLMELQEAVR-WTEMIRA 380
Cdd:PRK02224  547 AELEAEAEEKREAAAEAEEEAEEAREEVAElNSKLAELKERIESLERIR--TLLAAIADAEDEIERLREKREaLAELNDE 624


                  ...
gi 312836825  381 SRE 383
Cdd:PRK02224  625 RRE 627
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 277-371 3.09e-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: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  277 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLM 356
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                          90
                  ....*....|....*
gi 312836825  357 ERNQYKERLMELQEA 371
Cdd:COG1196   324 ELAELEEELEELEEE 338
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 265-329 3.14e-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: 3.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312836825  265 ETKNALNVVKNDLIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:COG4026   132 ELREELLELKEKIDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 252-397 3.16e-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: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   252 EVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAV-----------KQAKLKLEDKNRELEEELRKAR 320
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrdelKDYREKLEKLKREINELKRELD 409

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836825   321 AEAEDARQKakddddsdiptAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASRENPAMQEKKRSSIWQ 397
Cdd:TIGR02169  410 RLQEELQRL-----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE--WKLEQLAADLSKYEQELYD 473
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 249-378 3.53e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 40.12  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  249 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 328
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312836825  329 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 378
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-376 4.48e-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: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   260 NTQLLETKNALNVVK---NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKD---- 332
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnne 401

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 312836825   333 ---------------DDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTE 376
Cdd:TIGR02168  402 ierlearlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 292-389 5.92e-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: 5.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   292 QGELEAVKQAKLKLEDKNRELEEE--LRKARAEAEDARQKAKddddsdiptaQRKRFTRVEMARVLMERNQ--YKERLME 367
Cdd:pfam15709  365 QEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEE----------ERKQRLQLQAAQERARQQQeeFRRKLQE 434

                           90       100
                   ....*....|....*....|..
gi 312836825   368 LQEAVRWTEMIRASRENPAMQE 389
Cdd:pfam15709  435 LQRKKQQEEAERAEAEKQRQKE 456
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
 262-358 5.95e-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: 5.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   262 QLLETKNALNVVKNDLIAKVDELtceKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 341
Cdd:pfam09798    5 KLELLQQEKEKELEKLKNSYEEL---KSSHEEELEKLKQEVQKLEDEKKFLLNELRSLSATSPASSQSHETDTDDSSSVS 81

                           90
                   ....*....|....*..
gi 312836825   342 QRKRFTRVEMARVLMER 358
Cdd:pfam09798   82 LKKRKIEESTAESLKQK 98
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 92-337 6.51e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   92 QELSQPRSHTSLKDEL---------SDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGFvkgTDTSNKSEISKHIEV 162
Cdd:PLN03229  522 KRLSRAPNYLSLKYKLdmlnefsraKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEAL---KAEVASSGASSGDEL 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  163 QvaQETRNvSTESGENEEKSEVQAIIEStpeldMDKDLSGYKGSSTPT-KGIENKAFDRNTESLFEELSSAgsglIGDVD 241
Cdd:PLN03229  599 D--DDLKE-KVEKMKKEIELELAGVLKS-----MGLEVIGVTKKNKDTaEQTPPPNLQEKIESLNEEINKK----IERVI 666

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  242 EGADLLGMgreVENLILENTQLLETKNAlnvvknDLIAKVDELtcEKDVLQGELEAVKQAKLKleDKNRELEEELRKAR- 320
Cdd:PLN03229  667 RSSDLKSK---IELLKLEVAKASKTPDV------TEKEKIEAL--EQQIKQKIAEALNSSELK--EKFEELEAELAAARe 733

                         250
                  ....*....|....*...
gi 312836825  321 -AEAEDARQKAKDDDDSD 337
Cdd:PLN03229  734 tAAESNGSLKNDDDKEED 751
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 274-383 6.60e-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: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   274 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAED------ARQKAKDDDDSDIPTAQR--KR 345
Cdd:pfam01576  259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKREQEVTELKKalEE 338

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 312836825   346 FTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 383
Cdd:pfam01576  339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-380 6.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  227 EELSSAGSGLIGDVDEGADLLGMGREVENLILENTQLLETKNALNVVKndliAKVDELTCEKDVLQGELEAVKQAKLKLE 306
Cdd:COG4913   644 QERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE----EQLEELEAELEELEEELDELKGEIGRLE 719

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312836825  307 DKNRELEEELRKARAEAEDARQKAKDDDDSDIptaqRKRFTRVEMARVLME-RNQYKERLMELQEAVR--WTEMIRA 380
Cdd:COG4913   720 KELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERElRENLEERIDALRARLNraEEELERA 792
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-383 6.80e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  243 GADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAE 322
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312836825  323 AEDARQKAKDDDDSdipTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRwtEMIRASRE 383
Cdd:COG1196   367 LLEAEAELAEAEEE---LEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEE 422
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 159-276 7.83e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.79  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   159 HIEVQVAQ-ETRNVSTESGENEEKSEVQAIIESTPELDMDKD-LSGYKGSSTPTKGIENKAfDRNTESLFEELSS---AG 233
Cdd:pfam15905  195 HSKGKVAQlEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEqVEKYKLDIAQLEELLKEK-NDEIESLKQSLEEkeqEL 273

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 312836825   234 SGLIGDVDEGADLLgmGREVENLILE--------NTQLLETKNALNVVKND 276
Cdd:pfam15905  274 SKQIKDLNEKCKLL--ESEKEELLREyeekeqtlNAELEELKEKLTLEEQE 322
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 267-329 8.35e-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: 8.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312836825  267 KNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 220-394 8.89e-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: 40.43  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   220 RNTESLFEELSSAGSGLIGDVDEG-ADLLGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDV-------L 291
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEaeaeieeL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825   292 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAK-------DDDDSDIPTAQRKRFTRVEMARVLMERNQYKER 364
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          170       180       190
                   ....*....|....*....|....*....|.
gi 312836825   365 LMELQEAV-RWTEMIRASRENPAMQEKKRSS 394
Cdd:TIGR02168  868 IEELESELeALLNERASLEEALALLRSELEE 898
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
153-380 9.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  153 KSEISKHIEvqvAQETRNVSTESGENEEKSEVQAIIESTPELdmdKDLSGYKGSSTPTKGIENKAFD--RNTESLFEELS 230
Cdd:PRK03918  247 LESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKEL---KELKEKAEEYIKLSEFYEEYLDelREIEKRLSRLE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  231 SAGSGLIGDVDEGADLLGMGREVENLILE----------NTQLLETKNALNVVKNDLIAKVDELTCEKdvLQGELEAVKQ 300
Cdd:PRK03918  321 EEINGIEERIKELEEKEERLEELKKKLKElekrleeleeRHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEK 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  301 AKLKLEDKNRELEEELRKARAEAEDAR------QKAKddddSDIPTAQR-----------KRFTRvEMARVLMERNQYKE 363
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKELKkaieelKKAK----GKCPVCGRelteehrkellEEYTA-ELKRIEKELKEIEE 473

                         250
                  ....*....|....*..
gi 312836825  364 RLMELQEAVRWTEMIRA 380
Cdd:PRK03918  474 KERKLRKELRELEKVLK 490
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 277-329 9.66e-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: 9.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 312836825   277 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 329
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQER 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 275-417 9.84e-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: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312836825  275 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDArQKAKDDDDSDIPTAQRKrftrveMARV 354
Cdd:COG3883   115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-EAAKAELEAQQAEQEAL------LAQL 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312836825  355 LMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATKKPEPPV 417
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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