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Conserved domains on  [gi|568975822|ref|XP_006534280|]
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C-Jun-amino-terminal kinase-interacting protein 4 isoform X9 [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.
 806-1024 4.75e-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: 158.64  E-value: 4.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   806 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 883
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   884 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 963
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975822   964 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1024
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 258-326 7.26e-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: 107.40  E-value: 7.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822   258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 326
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 301-494 2.38e-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: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 380
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   381 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 458
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975822   459 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 494
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.
 806-1024 4.75e-41

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 158.64  E-value: 4.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   806 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 883
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   884 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 963
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975822   964 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1024
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 258-326 7.26e-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: 107.40  E-value: 7.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822   258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 326
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 301-494 2.38e-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: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 380
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   381 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 458
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975822   459 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 494
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-404 1.31e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  261 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 326
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822  327 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 404
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
271-385 1.78e-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: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  271 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 350
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975822  351 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 385
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
823-1020 2.44e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  823 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 895
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  896 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 968
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975822  969 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1020
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 219-338 2.77e-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: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  219 DRNTESLFEELSSAGSGLIGDVDE-----GADLlgEYSDHNFFGmgREVENLI-------LENTQ-LLETKNALNVVKND 285
Cdd:COG4026    68 DRVGRELAEKFFEELKGMVGHVERmklplGHDV--EYVDVELVR--KEIKNAIiraglksLQNIPeYNELREELLELKEK 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568975822  286 LIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 338
Cdd:COG4026   144 IDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-382 8.91e-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: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   260 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 330
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975822   331 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 382
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 ...
 301-342 1.28e-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: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975822  301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 342
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-401 1.96e-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: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   269 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 347
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   348 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 401
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
growth_prot_Scy NF041483
polarized growth protein Scy;
315-402 2.24e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  315 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 389
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975822  390 SRENPAMQEKKRS 402
Cdd:NF041483  344 EKLVAEAAEKART 356
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 258-387 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 568975822  258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 337
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975822  338 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 387
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.
 806-1024 4.75e-41

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


Pssm-ID: 465964  Cd Length: 487  Bit Score: 158.64  E-value: 4.75e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   806 EQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCL--HSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGVDG 883
Cdd:pfam19056   86 EEEEAVRAERTAKKPGPTICLGLEDGSISVYGSVDTAKKCLlqHFTPERSPVLCLKHSPQFLFAGLVNGKVAVYARAEDG 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   884 QWDLSNYHLLDLGrpHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDST 963
Cdd:pfam19056  166 LWDPEPPKLVKLG--VLPVRSLLALEDTVWASCGNQVTVISGETLQTEQSFEAHQDEGMSVSHMVVAGGGVWMAFSSGSS 243

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975822   964 LRLYHAHTYQHLQDVDIEPYVSKMLGtgklGFSFVRITALMVSCNRLWVGTGNGVIISIPL 1024
Cdd:pfam19056  244 IRLFHTETLEHLQDINIATRVHFMLP----GQKRVSVTSLLICQGLLWVGTNLGVIVALPV 300
JIP_LZII pfam16471
JNK-interacting protein leucine zipper II; This is the second leucine zipper domain (LZII) of ...
 258-326 7.26e-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: 107.40  E-value: 7.26e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822   258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR 326
Cdd:pfam16471    1 MGKEVENLIAENTELLATKNALNIVKDDLIARVDELSSEQEQLREELKALQAAKEKLKKRIKELEEELK 69
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 301-494 2.38e-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: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdiptaqRKRFTRVEMARVLMERNQYKERLmELQEA 380
Cdd:pfam17380  290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD----------RQAAIYAEQERMAMERERELERI-RQEER 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   381 VRWTEMIRasRENPAMQEKKRSSIwqFFSRLFSSSSNATKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKA-- 458
Cdd:pfam17380  359 KRELERIR--QEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArq 434

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568975822   459 --FDFLSEETEASLASRREQKREQYRQVKAHVQKEDGR 494
Cdd:pfam17380  435 reVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 283-392 5.00e-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: 5.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   283 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEE---LRKARAEAEDARQKAKDdddsdipTAQRKRFTRVE 359
Cdd:pfam20492    8 KQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERLEE-------SAEMEAEEKEQ 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 568975822   360 MARVLMERNQYKERLMEL-----QEAVRW-TEMIRASRE 392
Cdd:pfam20492   81 LEAELAEAQEEIARLEEEverkeEEARRLqEELEEAREE 119
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-404 1.31e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  261 EVENLILENTQLLETK----NALNVVKNDLIAKVDELTCEKDVL----------QGELEAVKQAKLKLEDKNRELEEELR 326
Cdd:PRK03918  190 NIEELIKEKEKELEEVlreiNEISSELPELREELEKLEKEVKELeelkeeieelEKELESLEGSKRKLEEKIRELEERIE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822  327 KARAEAEDARQKAKddddsDIPTAQRKRFTRVEMARvlmERNQYKERLMELQ-EAVRWTEMIRASRENPAMQEKKRSSI 404
Cdd:PRK03918  270 ELKKEIEELEEKVK-----ELKELKEKAEEYIKLSE---FYEEYLDELREIEkRLSRLEEEINGIEERIKELEEKEERL 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
271-385 1.78e-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: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  271 QLLETKNALNVVKNDLIAKVDELtcEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 350
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL 343

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568975822  351 QRK-RFTRVEMARVLMERNQYKERLMELQEAVRWTE 385
Cdd:COG4913   344 EREiERLERELEERERRRARLEALLAALGLPLPASA 379
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
823-1020 2.44e-04

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


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 45.37  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  823 TMWLGAQNGCLYVHS----SVAQWRKCLHSIKLKD-SILSIVHVK-GIVLVALADGTLAIFHRGvdgQWDLSNY-HLLDL 895
Cdd:COG3292   186 NLWIGTDGNGLYRLDpntgKFEHITHDPDPNSLSSnSIYSLFEDReGNLWVGTYGGGLNYLDPN---NSKFKSYrHNDPN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  896 GRPHHSIRCMTVVHD-----KVWCG-YRNKIYVVQPKAMKIeKSFDAHPRKESQVRQLAWVGDG-VWVSIRlDSTLRLYH 968
Cdd:COG3292   263 GLSGNSVRSIAEDSDgnlwiRLWIGtYGGGLFRLDPKTGKF-KRYNPNGLPSNSVYSILEDSDGnLWIGTS-GGGLYRYD 340

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975822  969 AHTYQhlqdvdIEPYvskmlgTGKLGFSFVRITALMV-SCNRLWVGTGNGVII 1020
Cdd:COG3292   341 PKTGK------FTKF------SEDNGLSNNFIRSILEdSDGNLWVGTNGGLYR 381
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 219-338 2.77e-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: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  219 DRNTESLFEELSSAGSGLIGDVDE-----GADLlgEYSDHNFFGmgREVENLI-------LENTQ-LLETKNALNVVKND 285
Cdd:COG4026    68 DRVGRELAEKFFEELKGMVGHVERmklplGHDV--EYVDVELVR--KEIKNAIiraglksLQNIPeYNELREELLELKEK 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568975822  286 LIAKVDE---LTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 338
Cdd:COG4026   144 IDEIAKEkekLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 303-401 2.96e-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: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   303 ELEAVKQA-KLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLmernqykERLMELQEAV 381
Cdd:pfam13868  233 QRQELQQArEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL-------EKQIEEREEQ 305

                           90       100
                   ....*....|....*....|
gi 568975822   382 RWTEMIRASRENPAMQEKKR 401
Cdd:pfam13868  306 RAAEREEELEEGERLREEEA 325
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 305-401 3.56e-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: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   305 EAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKddddsdiptaqrkrftrvEMArvlMERNQYKERLMEL-QEAVRW 383
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAE------------------ELE---EERRQAEEEAERLeQKRQEA 60

                           90
                   ....*....|....*...
gi 568975822   384 TEMIRASRENPAMQEKKR 401
Cdd:pfam20492   61 EEEKERLEESAEMEAEEK 78
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 258-380 4.05e-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: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 337
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568975822  338 KAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEA 380
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 301-342 4.08e-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: 4.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975822  301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 342
Cdd:COG0711    37 ADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKE 78
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
284-392 6.90e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  284 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDdddsdipTAQRKRFTRVEMARV 363
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES-------LQEEAEELQEELEEL 120

                          90       100
                  ....*....|....*....|....*....
gi 568975822  364 LMERNQYKERLMELQEAVRWTEMIRASRE 392
Cdd:COG4372   121 QKERQDLEQQRKQLEAQIAELQSEIAERE 149
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 260-401 7.08e-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: 7.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  260 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 339
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975822  340 KDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 401
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-382 8.91e-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: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   260 REVENLILENTQLLETKNALNVVK----NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELR-----KARA 330
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELeeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnlerqLEEL 321

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568975822   331 EAEDARQKAKDDDDSDIPTAQRKRFTRVEmARVLMERNQYKERLMELQEAVR 382
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 274-381 9.41e-04

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: 40.46  E-value: 9.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   274 ETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKlKLEDKNRELEEELRKARAEAEDARQKAKDDDdsdiptaqrk 353
Cdd:pfam04871    5 ELESEASSLKNENTELKAELQELSKQYNSLEQKESQAK-ELEAEVKKLEEALKKLKAELSEEKQKEKEKQ---------- 73

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568975822   354 rfTRVEMARVLM-----ERNQYKERLMELQEAV 381
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 ...
 301-342 1.28e-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: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568975822  301 QGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDD 342
Cdd:cd06503    36 AESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKE 77
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 260-396 1.46e-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: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  260 REVENLILENTQLLET-KNALNVVKNdliakVDELtcekDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 338
Cdd:COG1579    62 KRLELEIEEVEARIKKyEEQLGNVRN-----NKEY----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975822  339 AKD-DDDSDIPTAQRKRF---TRVEMARVLMERNQYKERLMElqEAVRWTEMIRASRENPAM 396
Cdd:COG1579   133 LAElEAELEEKKAELDEElaeLEAELEELEAEREELAAKIPP--ELLALYERIRKRKNGLAV 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 260-401 1.55e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   260 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQaklKLEDKNRELEEeLRKARAEAE---DAR 336
Cdd:pfam13868  145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQE---KAQDEKAERDE-LRAKLYQEEqerKER 220

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568975822   337 QKAKDDddsdiptAQRKRFTRVEMARVLMERNQYKERL--MELQEAVRWTEMIRAS----RENPAMQEKKR 401
Cdd:pfam13868  221 QKEREE-------AEKKARQRQELQQAREEQIELKERRlaEEAEREEEEFERMLRKqaedEEIEQEEAEKR 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-401 1.96e-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: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   269 NTQLLETKNALnvvkndliakvDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDI- 347
Cdd:TIGR02168  669 NSSILERRREI-----------EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAr 737

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   348 ------PTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKR 401
Cdd:TIGR02168  738 leaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 296-380 2.11e-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: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  296 EKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDipTAQRKRFTRV--EMARVLMERNQYKER 373
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--EEAQAEEYELlaELARLEQDIARLEER 310


                  ....*..
gi 568975822  374 LMELQEA 380
Cdd:COG1196   311 RRELEER 317
growth_prot_Scy NF041483
polarized growth protein Scy;
315-402 2.24e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.51  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  315 EDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA-----QRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRA 389
Cdd:NF041483  264 EQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAesaneQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEA 343

                          90
                  ....*....|...
gi 568975822  390 SRENPAMQEKKRS 402
Cdd:NF041483  344 EKLVAEAAEKART 356
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 286-380 2.89e-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: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  286 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLM 365
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                          90
                  ....*....|....*
gi 568975822  366 ERNQYKERLMELQEA 380
Cdd:COG1196   324 ELAELEEELEELEEE 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 261-406 2.96e-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: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   261 EVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAV-----------KQAKLKLEDKNRELEEELRKAR 329
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrdelKDYREKLEKLKREINELKRELD 409

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568975822   330 AEAEDARQKakddddsdiptAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEmiRASRENPAMQEKKRSSIWQ 406
Cdd:TIGR02169  410 RLQEELQRL-----------SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE--WKLEQLAADLSKYEQELYD 473
PRK14148 PRK14148
heat shock protein GrpE; Provisional
 258-387 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 568975822  258 MGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKdvlqgELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQ 337
Cdd:PRK14148    1 MSKQEKSNVEDKSLDIETAAQVETAQESASGALEELSVEE-----QLERAKDTIKELEDSCDQFKDEALRAKAEMENIRK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568975822  338 KAkdddDSDIPTAQR---KRFTRvEMARVLMERNQYKERLMELQEAVRWTEMI 387
Cdd:PRK14148   76 RA----ERDVSNARKfgiEKFAK-ELLPVIDSIEQALKHEVKLEEAIAMKEGI 123
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-385 4.33e-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: 41.58  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   269 NTQLLETKNALNVVK---NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKD---- 341
Cdd:TIGR02168  322 EAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnne 401

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568975822   342 ---------------DDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTE 385
Cdd:TIGR02168  402 ierlearlerledrrERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-379 4.88e-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: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   260 REVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKA 339
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 568975822   340 KddddsdiptAQRKRFTRVEM--ARVLMERNQYKERLMELQE 379
Cdd:TIGR02168  918 E---------ELREKLAQLELrlEGLEVRIDNLQERLSEEYS 950
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 301-398 5.39e-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: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   301 QGELEAVKQAKLKLEDKNRELEEE--LRKARAEAEDARQKAKddddsdiptaQRKRFTRVEMARVLMERNQ--YKERLME 376
Cdd:pfam15709  365 QEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEE----------ERKQRLQLQAAQERARQQQeeFRRKLQE 434

                           90       100
                   ....*....|....*....|..
gi 568975822   377 LQEAVRWTEMIRASRENPAMQE 398
Cdd:pfam15709  435 LQRKKQQEEAERAEAEKQRQKE 456
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
 271-367 6.05e-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: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   271 QLLETKNALNVVKNDLIAKVDELtceKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQKAKDDDDSDIPTA 350
Cdd:pfam09798    5 KLELLQQEKEKELEKLKNSYEEL---KSSHEEELEKLKQEVQKLEDEKKFLLNELRSLSATSPASSQSHETDTDDSSSVS 81

                           90
                   ....*....|....*..
gi 568975822   351 QRKRFTRVEMARVLMER 367
Cdd:pfam09798   82 LKKRKIEESTAESLKQK 98
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 283-392 6.11e-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: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822   283 KNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAED------ARQKAKDDDDSDIPTAQR--KR 354
Cdd:pfam01576  259 KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELRSKREQEVTELKKalEE 338

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568975822   355 FTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRE 392
Cdd:pfam01576  339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLE 376
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 276-338 7.66e-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: 7.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975822  276 KNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 338
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 286-338 9.27e-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: 9.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568975822   286 LIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK 338
Cdd:pfam06005    9 LETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQER 61
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 284-426 9.67e-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: 9.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  284 NDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDArQKAKDDDDSDIPTAQRKrftrveMARV 363
Cdd:COG3883   115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-EAAKAELEAQQAEQEAL------LAQL 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975822  364 LMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNATKKPEPPV 426
Cdd:COG3883   188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 271-381 9.68e-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: 39.14  E-value: 9.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975822  271 QLLETK-NALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEDKNRELEEELRKARAEAEDARQK---AKDDDD-- 344
Cdd:COG1579    13 QELDSElDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEye 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568975822  345 ---SDIPTAQRKR-FTRVEMARVLMERNQYKERLMELQEAV 381
Cdd:COG1579    93 alqKEIESLKRRIsDLEDEILELMERIEELEEELAELEAEL 133
 
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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