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Conserved domains on  [gi|568975820|ref|XP_006534279|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform X7 [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.
 820-1038 6.33e-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: 6.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   820 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 897
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   898 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 977
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975820   978 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1038
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 272-340 9.83e-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: 9.83e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820   272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 340
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 315-508 2.77e-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: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 394
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   395 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 472
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975820   473 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 508
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
 
Name Accession Description Interval E-value
WD40_2 pfam19056
WD40 repeated domain; This entry contains an array of WD40 repeats found in RhoGEF proteins.
 820-1038 6.33e-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: 6.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   820 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 897
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   898 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 977
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975820   978 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1038
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 272-340 9.83e-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: 9.83e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820   272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 340
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 315-508 2.77e-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: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 394
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   395 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 472
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975820   473 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 508
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-418 1.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  275 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 340
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820  341 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 418
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
285-399 1.81e-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: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  285 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 364
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975820  365 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 399
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
837-1034 2.47e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  837 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 909
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  910 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 982
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975820  983 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1034
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 233-352 3.07e-04

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 44.33  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  233 DRNTESLFEELSSAGSGLIGDVDE-----GADLlgEYSDHNFFGmgREVENLI-------LENTQ-LLETKNALNVVKND 299
Cdd:COG4026    68 DRVGRELAEKFFEELKGMVGHVERmklplGHDV--EYVDVELVR--KEIKNAIiraglksLQNIPeYNELREELLELKEK 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568975820  300 LIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 352
Cdd:COG4026   144 IDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-396 9.34e-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: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   274 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 344
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975820   345 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 396
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 ...
 315-356 1.33e-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: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975820  315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 356
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-553 2.07e-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: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   283 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 361
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   362 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 435
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   436 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 512
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568975820   513 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 553
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
growth_prot_Scy NF041483
polarized growth protein Scy;
329-416 2.37e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  329 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 403
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975820  404 SRENPAMQEKKRS 416
Cdd:NF041483  344 EKLVAEAAEKART 356
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 272-401 3.99e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 39.74  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 351
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975820  352 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 401
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.
 820-1038 6.33e-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: 6.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   820 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 897
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   898 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 977
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975820   978 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1038
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 272-340 9.83e-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: 9.83e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820   272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 340
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 315-508 2.77e-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: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 394
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   395 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 472
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975820   473 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 508
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 297-406 6.71e-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: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   297 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE---LRKARAEAEDARQKAKDdddsdipTAQRKRFTRVE 373
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEE-------SAEMEAEEKEQ 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568975820   374 MARVLMERNQYKERLMEL-----QEAVRW-TEMIRASRE 406
Cdd:pfam20492   81 LEAELAEAQEEIARLEEEverkeEEARRLqEELEEAREE 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-418 1.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  275 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 340
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820  341 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 418
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
285-399 1.81e-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: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  285 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 364
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975820  365 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 399
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
837-1034 2.47e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  837 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 909
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  910 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 982
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975820  983 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1034
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 233-352 3.07e-04

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


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 44.33  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  233 DRNTESLFEELSSAGSGLIGDVDE-----GADLlgEYSDHNFFGmgREVENLI-------LENTQ-LLETKNALNVVKND 299
Cdd:COG4026    68 DRVGRELAEKFFEELKGMVGHVERmklplGHDV--EYVDVELVR--KEIKNAIiraglksLQNIPeYNELREELLELKEK 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568975820  300 LIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 352
Cdd:COG4026   144 IDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 317-415 3.42e-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: 44.14  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   317 ELEAVKQA-KLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLmernqykERLMELQEAV 395
Cdd:pfam13868  233 QRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL-------EKQIEEREEQ 305

                           90       100
                   ....*....|....*....|
gi 568975820   396 RWTEMIRASRENPAMQEKKR 415
Cdd:pfam13868  306 RAAEREEELEEGERLREEEA 325
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-394 4.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 351
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568975820  352 KAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 394
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 315-356 4.29e-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: 4.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975820  315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 356
Cdd:COG0711    37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 319-415 4.50e-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: 41.06  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   319 EAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKddddsdiptaqrkrftrvEMArvlMERNQYKERLMEL-QEAVRW 397
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE------------------ELE---EERRQAEEEAERLeQKRQEA 60

                           90
                   ....*....|....*...
gi 568975820   398 TEMIRASRENPAMQEKKR 415
Cdd:pfam20492   61 EEEKERLEESAEMEAEEK 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 274-415 7.75e-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: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  274 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 353
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975820  354 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 415
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
298-406 7.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  298 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdipTAQRKRFTRVEMARV 377
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-------LQEEAEELQEELEEL 120

                          90       100
                  ....*....|....*....|....*....
gi 568975820  378 LMERNQYKERLMELQEAVRWTEMIRASRE 406
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-396 9.34e-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: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   274 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 344
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975820   345 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 396
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 288-395 1.22e-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: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   288 ETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKlKLEDKNRELEEELRKARAEAEDARQKAKDDDdsdiptaqrk 367
Cdd:pfam04871    5 ELESEASSLKNENTELKAELQELSKQYNSLEQKESQAK-ELEAEVKKLEEALKKLKAELSEEKQKEKEKQ---------- 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568975820   368 rfTRVEMARVLM-----ERNQYKERLMELQEAV 395
Cdd:pfam04871   74 --SELDDLLLLLgdleeKVEKYKARLKELGEEV 104
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 315-356 1.33e-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: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975820  315 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 356
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 274-410 1.68e-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: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  274 REVENLILENTQLLET-KNALNVVKNdliakVDELtcekDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 352
Cdd:COG1579    62 KRLELEIEEVEARIKKyEEQLGNVRN-----NKEY----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975820  353 AKD-DDDSDIPTAQRKRF---TRVEMARVLMERNQYKERLMElqEAVRWTEMIRASRENPAM 410
Cdd:COG1579   133 LAElEAELEEKKAELDEElaeLEAELEELEAEREELAAKIPP--ELLALYERIRKRKNGLAV 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 274-415 1.84e-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: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   274 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQaklKLEDKNRELEEeLRKARAEAE---DAR 350
Cdd:pfam13868  145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE---KAQDEKAERDE-LRAKLYQEEqerKER 220

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975820   351 QKAKDDddsdiptAQRKRFTRVEMARVLMERNQYKERL--MELQEAVRWTEMIRAS----RENPAMQEKKR 415
Cdd:pfam13868  221 QKEREE-------AEKKARQRQELQQAREEQIELKERRlaEEAEREEEEFERMLRKqaedEEIEQEEAEKR 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-553 2.07e-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: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   283 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 361
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   362 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATkk 435
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   436 peppvNLKYNAPTSHVTpSVKKRSSTLSQLPGDKSKAFDFLSEETE---ASLASRREQKREQYRQVKaHVQKEDGRVQAF 512
Cdd:TIGR02168  816 -----NEEAANLRERLE-SLERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELE-ALLNERASLEEA 888

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 568975820   513 GWSLPQKYKQVANGQGETKMKNLPVPVYLRPLDEKDASMKL 553
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-394 2.25e-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: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  310 EKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDipTAQRKRFTRV--EMARVLMERNQYKER 387
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELlaELARLEQDIARLEER 310


                  ....*..
gi 568975820  388 LMELQEA 394
Cdd:COG1196   311 RRELEER 317
growth_prot_Scy NF041483
polarized growth protein Scy;
329-416 2.37e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.12  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  329 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 403
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975820  404 SRENPAMQEKKRS 416
Cdd:NF041483  344 EKLVAEAAEKART 356
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 300-394 3.11e-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: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  300 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLM 379
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                          90
                  ....*....|....*
gi 568975820  380 ERNQYKERLMELQEA 394
Cdd:COG1196   324 ELAELEEELEELEEE 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 275-420 3.29e-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: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   275 EVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAV-----------KQAKLKLEDKNRELEEELRKAR 343
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrdelKDYREKLEKLKREINELKRELD 409

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975820   344 AEAEDARQKakddddsdiptAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASRENPAMQEKKRSSIWQ 420
Cdd:TIGR02169  410 RLQEELQRL-----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE--WKLEQLAADLSKYEQELYD 473
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 272-401 3.99e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172637 [Multi-domain]  Cd Length: 195  Bit Score: 39.74  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820  272 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 351
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975820  352 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 401
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-399 4.58e-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: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   283 NTQLLETKNALNVVK---NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKD---- 355
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnne 401

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568975820   356 ---------------DDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTE 399
Cdd:TIGR02168  402 ierlearlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-393 5.16e-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: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   274 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 353
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568975820   354 KddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 393
Cdd:TIGR02168  918 E---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
 285-381 6.13e-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: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   285 QLLETKNALNVVKNDLIAKVDELtceKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 364
Cdd:pfam09798    5 KLELLQQEKEKELEKLKNSYEEL---KSSHEEELEKLKQEVQKLEDEKKFLLNELRSLSATSPASSQSHETDTDDSSSVS 81

                           90
                   ....*....|....*..
gi 568975820   365 QRKRFTRVEMARVLMER 381
Cdd:pfam09798   82 LKKRKIEESTAESLKQK 98
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 315-412 6.37e-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: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   315 QGELEAVKQAKLKLEDKNRELEEE--LRKARAEAEDARQKAKddddsdiptaQRKRFTRVEMARVLMERNQ--YKERLME 390
Cdd:pfam15709  365 QEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEE----------ERKQRLQLQAAQERARQQQeeFRRKLQE 434

                           90       100
                   ....*....|....*....|..
gi 568975820   391 LQEAVRWTEMIRASRENPAMQE 412
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 ...
 297-406 6.92e-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: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975820   297 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAED------ARQKAKDDDDSDIPTAQR--KR 368
Cdd:pfam01576  259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKREQEVTELKKalEE 338

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568975820   369 FTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 406
Cdd:pfam01576  339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE 376
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 290-352 8.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 8.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975820  290 KNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 352
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 300-352 9.85e-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: 9.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568975820   300 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 352
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQER 61
 
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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