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Conserved domains on  [gi|1845974384|ref|NP_001370812|]
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UBX domain-containing protein 4 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 282-358 7.37e-36

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


:

Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 127.45  E-value: 7.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 282 RCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-252 2.96e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKALLEQKKQKDAEKKREADKHVK---EEMTKAREAKQERDAEAlvKAAKQRKMEKLAAESDKKRILAQIK 243
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEA--KAKAEAEAKAKAEEAKAKAEAAKAK 204


                  ....*....
gi 1845974384 244 ADREAAQKK 252
Cdd:TIGR02794 205 AAAEAAAKA 213
PRK05641 super family cl35354
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 85-159 7.22e-05

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


The actual alignment was detected with superfamily member PRK05641:

Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 42.93  E-value: 7.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974384  85 NGKPLEVITPLVGKtyDQFRAKFDKATAQFVN---GMPTAA-ANQLSTPSPSPAPVQVPASTdaPIPAPTPVTAPIQSS 159
Cdd:PRK05641    9 DGVEYEVEVEELGP--GKFRVSFEGKTYEVEAkglGIDLSAvQEQVPTPAPAPAPAVPSAPT--PVAPAAPAPAPASAG 83
 
Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 282-358 7.37e-36

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 127.45  E-value: 7.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 282 RCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 282-358 3.92e-29

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 109.32  E-value: 3.92e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384  282 RCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVSAALGDGNDPFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 279-358 5.02e-28

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 106.22  E-value: 5.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 279 PSDRCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:pfam00789   1 AEDVTRLQIRLPDGSRLVRRFNSSDKLQTVYDFVDSNRYDDLEPFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLEP 80
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-252 2.96e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKALLEQKKQKDAEKKREADKHVK---EEMTKAREAKQERDAEAlvKAAKQRKMEKLAAESDKKRILAQIK 243
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEA--KAKAEAEAKAKAEEAKAKAEAAKAK 204


                  ....*....
gi 1845974384 244 ADREAAQKK 252
Cdd:TIGR02794 205 AAAEAAAKA 213
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 164-252 9.18e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 9.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 164 EMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEE----MTKAREAKQERDAEALVKAAKQRKmEKLAAESDKK-RI 238
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEaeaaKKAAAEAKKKAEAEAAAKAAAEAK-KKAEAEAKKKaAA 213

                          90
                  ....*....|....
gi 1845974384 239 LAQIKADREAAQKK 252
Cdd:PRK09510  214 EAKKKAAAEAKAAA 227
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
157-274 2.24e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 157 QSSSTSQEMTRELAEKVARAKALLEQKKQKD----------AEKKREADKHVKEEMTKAREAKQERDAE-ALVKAAKQRK 225
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRdelneelkelAEKRDELNAQVKELREEAQELREKRDELnEKVKELKEER 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1845974384 226 MEKLAAESDKKRILAQIKADREAAQKKFGKLVNTENASENTEKKQETTV 274
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 163-252 7.14e-05

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: 44.91  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKDAEKKREADKHV------KEEMTKAREAKQERdaealVKAAKQRKMEKLAA----E 232
Cdd:pfam13868 122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleylkeKAEREEEREAEREE-----IEEEKEREIARLRAqqekA 196

                          90       100
                  ....*....|....*....|
gi 1845974384 233 SDKKRILAQIKADREAAQKK 252
Cdd:pfam13868 197 QDEKAERDELRAKLYQEEQE 216
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 85-159 7.22e-05

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 42.93  E-value: 7.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974384  85 NGKPLEVITPLVGKtyDQFRAKFDKATAQFVN---GMPTAA-ANQLSTPSPSPAPVQVPASTdaPIPAPTPVTAPIQSS 159
Cdd:PRK05641    9 DGVEYEVEVEELGP--GKFRVSFEGKTYEVEAkglGIDLSAvQEQVPTPAPAPAPAVPSAPT--PVAPAAPAPAPASAG 83
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 177-252 9.50e-04

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: 39.34  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 177 KALLEQKKQK------DAEKKR-EADKHVKEEMTKAREAKQERD---AEALVKAAKQRKMEKLAAESDKKRILAQIKADR 246
Cdd:cd06503    25 LKALDEREEKiaesleEAEKAKeEAEELLAEYEEKLAEARAEAQeiiEEARKEAEKIKEEILAEAKEEAERILEQAKAEI 104


                  ....*.
gi 1845974384 247 EAAQKK 252
Cdd:cd06503   105 EQEKEK 110
growth_prot_Scy NF041483
polarized growth protein Scy;
160-249 1.26e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  160 STSQEMTRELAEKVAR--------AKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAK--------- 222
Cdd:NF041483   301 SANEQRTRTAKEEIARlvgeatkeAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARtaeevltka 380

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1845974384  223 ----QRKMEKLAAESDKKRILAQIKADR---EAA 249
Cdd:NF041483   381 sedaKATTRAAAEEAERIRREAEAEADRlrgEAA 414
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 158-332 5.78e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  158 SSSTSQEMTRELAEKVARAkalLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKR 237
Cdd:PTZ00108  1122 KNTTPKDMWLEDLDKFEEA---LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNS 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  238 ILAQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKAVPSDRCRLQVRLPDGSTFVEEFPSNDVlnSLVEIIRQKPS 317
Cdd:PTZ00108  1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDL--SKEGKPKNAPK 1276

                          170
                   ....*....|....*
gi 1845974384  318 IAGTTFEIQQPYPRR 332
Cdd:PTZ00108  1277 RVSAVQYSPPPPSKR 1291
 
Name Accession Description Interval E-value
UBX_UBXN4 cd16117
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; ...
 282-358 7.37e-36

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 4 (UBXN4) and similar proteins; UBXN4, also termed ERAD (endoplasmic-reticulum-associated protein degradation) substrate erasing protein (erasin), or UBX domain-containing protein 2 (UBXD2), or UBXDC1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN4 is an endoplasmic reticulum (ER) localized protein that interacts with p97 (also known as VCP or Cdc48) via its UBX domain. Erasin exists in a complex with other p97/VCP-associated factors involved in endoplasmic-reticulum-associated protein degradation (ERAD). p97 is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The overexpression of UBXN4 increases degradation of a classical ERAD substrate and UBXN4 levels are increased in ER stressed cells. Anti-UBXN4 staining is increased in neuropathological lesions in brains of patients with Alzheimer's disease.


Pssm-ID: 340534 [Multi-domain]  Cd Length: 77  Bit Score: 127.45  E-value: 7.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 282 RCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:cd16117     1 TARIQFRLPDGSSFTNQFPSDAPLEEARQFVAQTVGPAYGPFSLATTFPRREFTDDDYQKTLLELELAPSAALVVLP 77
UBX smart00166
Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.
 282-358 3.92e-29

Domain present in ubiquitin-regulatory proteins; Present in FAF1 and Shp1p.


Pssm-ID: 197552 [Multi-domain]  Cd Length: 77  Bit Score: 109.32  E-value: 3.92e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384  282 RCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:smart00166   1 VCRLQIRLPDGSRLVRRFPSSDTLRTVYEFVSAALGDGNDPFTLNSPFPRRTFTKDDYSKKLLELALLPSSTLVLEP 77
UBX pfam00789
UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general ...
 279-358 5.02e-28

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.


Pssm-ID: 395637 [Multi-domain]  Cd Length: 80  Bit Score: 106.22  E-value: 5.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 279 PSDRCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQ 358
Cdd:pfam00789   1 AEDVTRLQIRLPDGSRLVRRFNSSDKLQTVYDFVDSNRYDDLEPFSLNTPFPRRPLTDLDYSKTLKEAGLLPNSTLVLEP 80
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
 284-356 1.09e-19

Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain.


Pssm-ID: 340466 [Multi-domain]  Cd Length: 74  Bit Score: 83.08  E-value: 1.09e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845974384 284 RLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVV 356
Cdd:cd01767     1 RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNLGDSPSSFSLVTSFPRRVLTDEDSDKTLEELGLTPNAVLFV 73
UBX_UBXN1 cd01772
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; ...
 281-356 7.61e-14

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 1 (UBXN1) and similar proteins; UBXN1, also termed SAPK substrate protein 1 (SAKS1), UBA/UBX 33.3 kDa protein (Y33K), or UBXD10, is a widely expressed protein containing an N-terminal ubiquitin-associated (UBA) domain, a coiled-coil region, and a C-terminal ubiquitin-like (Ubl or UBX) domain that has a beta-grasp ubiquitin-like fold without the C-terminal double glycine motif. UBXN1 has been identified as a substrate for stress-activated protein kinases (SAPKs). It binds polyubiquitin and valosin-containing protein (VCP), suggesting a role as an adaptor that directs VCP to polyubiquitinated proteins facilitating its destruction by the proteasome. In addition, UBXN1 specifically binds to Homer2b. It may also interact with ubiquitin (Ub) and be involved in the Ub-proteasome proteolytic pathways. UBXN1 can also associate with autoubiquitinated BRCA1 tumor suppressor and inhibit its enzymatic function through its UBA domains.


Pssm-ID: 340470 [Multi-domain]  Cd Length: 81  Bit Score: 66.57  E-value: 7.61e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974384 281 DRCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVV 356
Cdd:cd01772     5 DECRLQVRLTNGSTLTQTFGAKEQLAAVRLYVELNRTDGDGPFSLMTTFPRKVFTEEDMEKPLKELGLVPSAVLIV 80
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-252 2.96e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.16  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKALLEQKKQKDAEKKREADKHVK---EEMTKAREAKQERDAEAlvKAAKQRKMEKLAAESDKKRILAQIK 243
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKaaaEAKKKAEEAKKKAEAEA--KAKAEAEAKAKAEEAKAKAEAAKAK 204


                  ....*....
gi 1845974384 244 ADREAAQKK 252
Cdd:TIGR02794 205 AAAEAAAKA 213
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 164-252 9.18e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 9.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 164 EMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEE----MTKAREAKQERDAEALVKAAKQRKmEKLAAESDKK-RI 238
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEaeaaKKAAAEAKKKAEAEAAAKAAAEAK-KKAEAEAKKKaAA 213

                          90
                  ....*....|....
gi 1845974384 239 LAQIKADREAAQKK 252
Cdd:PRK09510  214 EAKKKAAAEAKAAA 227
PTZ00121 PTZ00121
MAEBL; Provisional
 166-271 2.18e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 2.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  166 TRELAEKVARAKALLEQKKQKD-AEKKREADKHVKEEMTKAREAKQERDaEALVKAAKQRKMEKLAAESDKKRILAQIKA 244
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKADeAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451

                           90       100
                   ....*....|....*....|....*..
gi 1845974384  245 DREAAQKkfgklvnTENASENTEKKQE 271
Cdd:PTZ00121  1452 KAEEAKK-------AEEAKKKAEEAKK 1471
PTZ00121 PTZ00121
MAEBL; Provisional
 162-271 2.70e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  162 SQEMTRELAEKVARA--KALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDaEALVKAAKQRKMEKLAAESDKKRIL 239
Cdd:PTZ00121  1368 AAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKA 1446

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1845974384  240 AQIKADREAAQKkfgklvntenaSENTEKKQE 271
Cdd:PTZ00121  1447 DEAKKKAEEAKK-----------AEEAKKKAE 1467
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 170-264 6.61e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 170 AEKVARAKALLEQKKQKDAEKKREAD-----KHVKEEMTKAR-EAKQERDAEALVKAAKQRKMEKLAAESDKKRilaqiK 243
Cdd:PRK09510  163 AAAEAKKKAEAEAAKKAAAEAKKKAEaeaaaKAAAEAKKKAEaEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA-----A 237

                          90       100
                  ....*....|....*....|.
gi 1845974384 244 ADREAAQKKFGKLVNTENASE 264
Cdd:PRK09510  238 AEKAAAAKAAEKAAAAKAAAE 258
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 117-252 9.51e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.53  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 117 GMPTAAANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSsstsQEMTRELAEKVARAKALL---EQKKQKDAEKKRE 193
Cdd:TIGR02794  46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAE----QARQKELEQRAAAEKAAKqaeQAAKQAEEKQKQA 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845974384 194 ADKHVKEEMTKAREAKQERDAEALVKAAKQRKME---KLAAESDKKRILAQIKADREAAQKK 252
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEakaKAAAEAKKKAEEAKKKAEAEAKAKA 183
PTZ00121 PTZ00121
MAEBL; Provisional
 168-271 9.62e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 9.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQE----RDAEALVKAAKQ-RKMEKLAAESDKKRILAQI 242
Cdd:PTZ00121  1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaeeaKKAEEAKKKAEEaKKADEAKKKAEEAKKADEA 1488

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1845974384  243 KADREAAQKKFGKLVNTENASENTE--KKQE 271
Cdd:PTZ00121  1489 KKKAEEAKKKADEAKKAAEAKKKADeaKKAE 1519
PTZ00121 PTZ00121
MAEBL; Provisional
 170-271 1.54e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  170 AEKVARAKALLEQKKQKDAEKKREADKHVKEEMTK-----AREAKQERDAEALVKAAKQRKMEklaAESDKKRILAQIKA 244
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkadaaKKKAEEKKKADEAKKKAEEDKKK---ADELKKAAAAKKKA 1420

                           90       100
                   ....*....|....*....|....*..
gi 1845974384  245 DReaAQKKFGKLVNTENASENTEKKQE 271
Cdd:PTZ00121  1421 DE--AKKKAEEKKKADEAKKKAEEAKK 1445
UBX_UBXN3A cd01771
Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as ...
 283-356 2.05e-05

Ubiquitin regulatory domain X (UBX) found in FAS associated factor 1 (FAF1, also known as UBXN3A) and similar proteins; UBX domain-containing protein 3A (UBXN3A),also termed UBX domain-containing protein 12 (UBXD12), or FAF1, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, FAF1 contains two tandem ubiquitin-like (Ubl) domains, which shows high structural similarity with UBX domain. FAF1 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The FAF1-p97 complex inhibits the proteasomal protein degradation in which p97 acts as a co-chaperone. Moreover, FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway. This family corresponds to UBX domain.


Pssm-ID: 340469  Cd Length: 80  Bit Score: 42.60  E-value: 2.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974384 283 CRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQK--PSiagTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVV 356
Cdd:cd01771     5 SKLRFRLPGGEFLTRRFLASEPLQVLLNFVASKgyPP---DEYKLLTTFPRRDLTQLDPSKTLEELKLFPQETLFL 77
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
157-274 2.24e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.06  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 157 QSSSTSQEMTRELAEKVARAKALLEQKKQKD----------AEKKREADKHVKEEMTKAREAKQERDAE-ALVKAAKQRK 225
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRdelneelkelAEKRDELNAQVKELREEAQELREKRDELnEKVKELKEER 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1845974384 226 MEKLAAESDKKRILAQIKADREAAQKKFGKLVNTENASENTEKKQETTV 274
Cdd:COG1340    81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV 129
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 163-278 2.52e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARakallEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQI 242
Cdd:PRK09510   86 QQQAEELQQKQAA-----EQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845974384 243 KADREAAQKKFGKLVNTENASENTEKKQETTVGKAV 278
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAA 196
PTZ00121 PTZ00121
MAEBL; Provisional
 168-271 6.80e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAK---QERDAEALVKAAKQRKMEKL--AAESDKKRILAQI 242
Cdd:PTZ00121  1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELkkAEELKKAEEKKKA 1566

                           90       100
                   ....*....|....*....|....*....
gi 1845974384  243 KADREAAQKKFGKLVNTENASENTEKKQE 271
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 163-252 7.14e-05

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: 44.91  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKDAEKKREADKHV------KEEMTKAREAKQERdaealVKAAKQRKMEKLAA----E 232
Cdd:pfam13868 122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIleylkeKAEREEEREAEREE-----IEEEKEREIARLRAqqekA 196

                          90       100
                  ....*....|....*....|
gi 1845974384 233 SDKKRILAQIKADREAAQKK 252
Cdd:pfam13868 197 QDEKAERDELRAKLYQEEQE 216
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 85-159 7.22e-05

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 42.93  E-value: 7.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1845974384  85 NGKPLEVITPLVGKtyDQFRAKFDKATAQFVN---GMPTAA-ANQLSTPSPSPAPVQVPASTdaPIPAPTPVTAPIQSS 159
Cdd:PRK05641    9 DGVEYEVEVEELGP--GKFRVSFEGKTYEVEAkglGIDLSAvQEQVPTPAPAPAPAVPSAPT--PVAPAAPAPAPASAG 83
PTZ00121 PTZ00121
MAEBL; Provisional
 170-284 7.23e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  170 AEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADREAA 249
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1845974384  250 QKKFGKLVNTENASENTEKKQETTVGKAVPSDRCR 284
Cdd:PTZ00121  1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
PTZ00121 PTZ00121
MAEBL; Provisional
 168-278 7.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 7.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKME----KLAAESDKKRIlAQIK 243
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKA-EEAK 1750

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1845974384  244 ADREAAQKKFGKLVNTENASENTEKKQETTVGKAV 278
Cdd:PTZ00121  1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
UBX_UBXN7 cd01773
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; ...
 283-356 8.32e-05

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding.


Pssm-ID: 340471  Cd Length: 76  Bit Score: 40.69  E-value: 8.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845974384 283 CRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKpSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVV 356
Cdd:cd01773     2 SKLMLRFPDGKREQLSLPASAKLKALVKYVSSK-GYPNERYELVTNFPRRKLSHLDYDITLKEAGLCPQETIFV 74
PTZ00121 PTZ00121
MAEBL; Provisional
 168-277 9.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 9.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAE-KKREADKHVKEEMTKAREAKQERDAEALVKAA--KQRKMEKLAAESDKKRILAQIKA 244
Cdd:PTZ00121  1630 EEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEedEKKAAEALKKEAEEAKKAEELKK 1709

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1845974384  245 DREAAQKKFGKLVNTENA----SENTEKKQETTVGKA 277
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKA 1746
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
164-274 1.00e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.48  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 164 EMTRElaEKVARAKALLEQKKQKdAEKKREADKhvkeemtkaREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIK 243
Cdd:COG2268   196 EIIRD--ARIAEAEAERETEIAI-AQANREAEE---------AELEQEREIETARIAEAEAELAKKKAEERREAETARAE 263

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974384 244 ADREAAQKKFGKLVNTENASENTEKKQETTV 274
Cdd:COG2268   264 AEAAYEIAEANAEREVQRQLEIAEREREIEL 294
PTZ00121 PTZ00121
MAEBL; Provisional
 170-277 1.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  170 AEKVARAKALLEQKKQKDAEKKREADKHVKEEmtKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADREAA 249
Cdd:PTZ00121  1184 AEEVRKAEELRKAEDARKAEAARKAEEERKAE--EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261

                           90       100
                   ....*....|....*....|....*...
gi 1845974384  250 QKKFGKLVNTENASentEKKQETTVGKA 277
Cdd:PTZ00121  1262 MAHFARRQAAIKAE---EARKADELKKA 1286
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 170-260 1.19e-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: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 170 AEKV-ARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKAD--- 245
Cdd:COG0711    43 AERAkEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEvad 122

                          90
                  ....*....|....*..
gi 1845974384 246 --REAAQKKFGKLVNTE 260
Cdd:COG0711   123 laVAIAEKILGKELDAA 139
PTZ00121 PTZ00121
MAEBL; Provisional
 168-271 1.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQErdAEALVKAAKQRKMEKLAAESDKKRILAQIKADRE 247
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK--ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                           90       100
                   ....*....|....*....|....
gi 1845974384  248 AAQKKFGKLVNTENASENTEKKQE 271
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKKKAE 1388
UBX_UBXN11 cd17077
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ...
 281-356 1.39e-04

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN11 may function as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation.


Pssm-ID: 340597  Cd Length: 76  Bit Score: 40.28  E-value: 1.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 281 DRCRLQVRLPDGS-TFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFtnDDYSKTFLENQLTPSTALVV 356
Cdd:cd17077     1 DVTTLRIKSENGEqTYILKMRFSDTIGDLRRYLDKHRSKDAASYEIVTTFPNKVY--DDDSATLEELGLVPNATLHL 75
PTZ00121 PTZ00121
MAEBL; Provisional
 168-277 1.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKR--EADKHVKEEMTKAREAKQE---RDAEALVKAAKQRKMEKLAAESDKKRILAQI 242
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1845974384  243 KADreAAQKKFGKLVNTENASENTE--KKQETTVGKA 277
Cdd:PTZ00121  1379 KAD--AAKKKAEEKKKADEAKKKAEedKKKADELKKA 1413
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 170-282 1.67e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 170 AEKVARAKALLE-QKKQKDAEKKREADKHVKEEMTK--AREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADR 246
Cdd:TIGR02794 152 AEEEAKAKAAAEaKKKAEEAKKKAEAEAKAKAEAEAkaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845974384 247 EAAQKKFGKlvntenASENTEKKQETTVGKAVPSDR 282
Cdd:TIGR02794 232 AELGDIFGL------ASGSNAEKQGGARGAAAGSEV 261
PTZ00121 PTZ00121
MAEBL; Provisional
 163-277 1.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  163 QEMTRELAEKVARA---KALLEQKKQKDAEKKREAdkhvkEEMTKAREAKQERDAEALVKAAK-QRKMEKL-AAESDKKR 237
Cdd:PTZ00121  1615 AEEAKIKAEELKKAeeeKKKVEQLKKKEAEEKKKA-----EELKKAEEENKIKAAEEAKKAEEdKKKAEEAkKAEEDEKK 1689

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1845974384  238 ILAQIKADREAAQKkfgklvntenaSENTEKKQETTVGKA 277
Cdd:PTZ00121  1690 AAEALKKEAEEAKK-----------AEELKKKEAEEKKKA 1718
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 123-252 1.71e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 123 ANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKALLEQKKQKDAEK---KREADKHVK 199
Cdd:TIGR02794  56 QQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEakaKQAAEAKAK 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845974384 200 EE----MTKAREAKQERDAEALVKAA-----KQRKMEKLAAESDKKRILAQIKADREAAQKK 252
Cdd:TIGR02794 136 AEaeaeRKAKEEAAKQAEEEAKAKAAaeakkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
PTZ00121 PTZ00121
MAEBL; Provisional
 168-277 1.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQE----RDAEALVKAAKQRKMEklaAESDKKRILAQIK 243
Cdd:PTZ00121  1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeaKKADEAKKKAEEAKKK---ADEAKKAAEAKKK 1511

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1845974384  244 AD--REAAQ-KKFGKLVNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1512 ADeaKKAEEaKKADEAKKAEEAKKADEAKKAEEKKKA 1548
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-271 1.94e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 170 AEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEklAAESDKKRILAQIKADREAA 249
Cdd:COG1196   209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--AELEELRLELEELELELEEA 286

                          90       100
                  ....*....|....*....|..
gi 1845974384 250 QKKFGKLVNTENASENTEKKQE 271
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLE 308
PTZ00121 PTZ00121
MAEBL; Provisional
 168-277 2.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQK-DAEKKREADKHVKEEMTKAREAKQERDAEALVKAAK---------QRKMEKLAAESDKKR 237
Cdd:PTZ00121  1312 EEAKKADEAKKKAEEAKKKaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkkeeaKKKADAAKKKAEEKK 1391

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1845974384  238 ILAQIKADREAAQKKFGKLVNTENASENTE--KKQETTVGKA 277
Cdd:PTZ00121  1392 KADEAKKKAEEDKKKADELKKAAAAKKKADeaKKKAEEKKKA 1433
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 167-268 2.51e-04

Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 40.28  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKallEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEAlvkaakqRKmeklAAESDKKRILAQIKADR 246
Cdd:COG2811    15 EEADEIIEEAK---EEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEA-------RE----EAEAEAEEIIEEGEKEA 80

                          90       100
                  ....*....|....*....|..
gi 1845974384 247 EAAQKKfgklvntenASENTEK 268
Cdd:COG2811    81 EALKKK---------AEDKLDK 93
PTZ00121 PTZ00121
MAEBL; Provisional
 164-277 3.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  164 EMTRELAEKVARA----KALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEAlvKAAKQRKMEKLAAESDKKRIL 239
Cdd:PTZ00121  1421 DEAKKKAEEKKKAdeakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKK 1498

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1845974384  240 AQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
PTZ00121 PTZ00121
MAEBL; Provisional
 164-277 3.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  164 EMTRELAEK-VARAKALLEQKKQKDAE--KKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILA 240
Cdd:PTZ00121  1584 EEAKKAEEArIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1845974384  241 QIKADREAAQKKfgKLVNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1664 AEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEA 1698
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 56-155 3.89e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 42.16  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  56 KLKAGETSAQQFAD----IYPTPILPAAylIDQNGKPLEVITPLVGKTYDQFRAKFDKATAQFVNGM------PTAAANQ 125
Cdd:PHA02682   15 KLVLADTSSSLFTKcpqaTIPAPAAPCP--PDADVDPLDKYSVKEAGRYYQSRLKANSACMQRPSGQsplapsPACAAPA 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1845974384 126 LSTPSPSPAPVQVPASTDAPIPAPTPVTAP 155
Cdd:PHA02682   93 PACPACAPAAPAPAVTCPAPAPACPPATAP 122
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 162-236 4.90e-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: 39.90  E-value: 4.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 162 SQEMTRELAE--KVARAKALLEQKKQKDAEKKREadkhvKEEMTKAREAKqERDAEALVKAAKQRKMEKLAAESDKK 236
Cdd:pfam20492  32 SEETAEELEEerRQAEEEAERLEQKRQEAEEEKE-----RLEESAEMEAE-EKEQLEAELAEAQEEIARLEEEVERK 102
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 163-271 4.97e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKvaRAKALLEQKKQKDAEKK-READKHVKEEMTKAREA---KQERDAEALVKAAKQrkmeklAAESDKKRI 238
Cdd:PRK09510  100 QERLKQLEKE--RLAAQEQKKQAEEAAKQaALKQKQAEEAAAKAAAAakaKAEAEAKRAAAAAKK------AAAEAKKKA 171

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974384 239 LAQIKADREAAQKKFGKLVNTENASENTEKKQE 271
Cdd:PRK09510  172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
PTZ00121 PTZ00121
MAEBL; Provisional
 164-277 5.85e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 5.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  164 EMTRELAEKVARA-----KALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEAlvKAAKQRKMEKLAAESDKKRI 238
Cdd:PTZ00121  1381 DAAKKKAEEKKKAdeakkKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK--KAEEAKKADEAKKKAEEAKK 1458

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1845974384  239 LAQIKADREAAQK--KFGKLVNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1459 AEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKKKA 1499
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 156-255 6.54e-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: 41.83  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 156 IQSSSTSQEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERD--AEALVK----AAKQRKMEKL 229
Cdd:pfam13868  15 LLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKryRQELEEqieeREQKRQEEYE 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 1845974384 230 AAESDKKRILAQIKA----DREAAQKKFGK 255
Cdd:pfam13868  95 EKLQEREQMDEIVERiqeeDQAEAEEKLEK 124
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 156-270 6.71e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 156 IQSSSTSQemtRELAEKVARAKALL---EQKKQKDAEKKREADKHVKEEMtkareAKQERDAEALVKAAKQRKMEKLAA- 231
Cdd:PRK00409  522 IASLEELE---RELEQKAEEAEALLkeaEKLKEELEEKKEKLQEEEDKLL-----EEAEKEAQQAIKEAKKEADEIIKEl 593

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1845974384 232 -ESDKKRILAQIKADREAAQKKFGKlvntenASENTEKKQ 270
Cdd:PRK00409  594 rQLQKGGYASVKAHELIEARKRLNK------ANEKKEKKK 627
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 163-251 6.75e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 6.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEkvARAKALLEQKKQKDAEKKREADKHVKEEMTKAR----------EAKQERDAEALVKAAKQRKMEKLAAE 232
Cdd:PRK09510  114 QEQKKQAEE--AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRaaaaakkaaaEAKKKAEAEAAKKAAAEAKKKAEAEA 191

                          90
                  ....*....|....*....
gi 1845974384 233 SDKKRILAQIKADREAAQK 251
Cdd:PRK09510  192 AAKAAAEAKKKAEAEAKKK 210
PTZ00121 PTZ00121
MAEBL; Provisional
 168-252 7.00e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 7.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLE-QKKQKDAEKKREADKHVKEEMTKAREAK---QERDAEALVKAAKQRKMEKLAAESDKKRILAQIK 243
Cdd:PTZ00121  1474 EAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAKKKADEAKkaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553

                           90
                   ....*....|.
gi 1845974384  244 AD--REAAQKK 252
Cdd:PTZ00121  1554 AEelKKAEEKK 1564
PLN02316 PLN02316
synthase/transferase
 189-274 7.85e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 42.16  E-value: 7.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  189 EKKREADKHVKEEMTKAREAKQERDAEAlvkaakqrkmEKLAAESDKKRILAQIKADREAAQKKFGK-LVNTENA--SEN 265
Cdd:PLN02316   253 EKRRELEKLAKEEAERERQAEEQRRREE----------EKAAMEADRAQAKAEVEKRREKLQNLLKKaSRSADNVwyIEP 322


                   ....*....
gi 1845974384  266 TEKKQETTV 274
Cdd:PLN02316   323 SEFKAGDTV 331
PTZ00121 PTZ00121
MAEBL; Provisional
 168-277 8.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 8.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKD-AEKKREADKHVKEEMTKAREAKQErdAEALVKAAKQRKMEKLAAESDKKRilaqiKAD- 245
Cdd:PTZ00121  1454 EEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAKKAEEAK-----KADe 1526

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1845974384  246 -REAAQKKfgklvNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1527 aKKAEEAK-----KADEAKKAEEKKKADELKKA 1554
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 177-252 9.50e-04

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: 39.34  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 177 KALLEQKKQK------DAEKKR-EADKHVKEEMTKAREAKQERD---AEALVKAAKQRKMEKLAAESDKKRILAQIKADR 246
Cdd:cd06503    25 LKALDEREEKiaesleEAEKAKeEAEELLAEYEEKLAEARAEAQeiiEEARKEAEKIKEEILAEAKEEAERILEQAKAEI 104


                  ....*.
gi 1845974384 247 EAAQKK 252
Cdd:cd06503   105 EQEKEK 110
PTZ00121 PTZ00121
MAEBL; Provisional
 170-277 1.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  170 AEKVARAKallEQKKQKDAeKKREADKHVKEEMTKAREAKQERDAEALVKAAKqRKMEKLAAESDKKRILAQIKADREAA 249
Cdd:PTZ00121  1280 ADELKKAE---EKKKADEA-KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEA 1354

                           90       100
                   ....*....|....*....|....*...
gi 1845974384  250 QKKfgKLVNTENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1355 AAD--EAEAAEEKAEAAEKKKEEAKKKA 1380
PTZ00121 PTZ00121
MAEBL; Provisional
 170-277 1.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  170 AEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKA---REAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADR 246
Cdd:PTZ00121  1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1845974384  247 EAAQKKFGKLvntENASENTEKKQETTVGKA 277
Cdd:PTZ00121  1325 EEAKKKADAA---KKKAEEAKKAAEAAKAEA 1352
PTZ00121 PTZ00121
MAEBL; Provisional
 168-271 1.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  168 ELAEKVARAKALLEQKKQKDAEKKR--EADKHVKEEMTKAREAKQ----ERDAEALVKAAKQRKMEKLAAESDKKRILAQ 241
Cdd:PTZ00121  1460 EEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKaaeaKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1845974384  242 IKAD--REAAQ-KKFGKLVNTENASENTEKKQE 271
Cdd:PTZ00121  1540 KKAEekKKADElKKAEELKKAEEKKKAEEAKKA 1572
growth_prot_Scy NF041483
polarized growth protein Scy;
160-249 1.26e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 41.35  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  160 STSQEMTRELAEKVAR--------AKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAK--------- 222
Cdd:NF041483   301 SANEQRTRTAKEEIARlvgeatkeAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARtaeevltka 380

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1845974384  223 ----QRKMEKLAAESDKKRILAQIKADR---EAA 249
Cdd:NF041483   381 sedaKATTRAAAEEAERIRREAEAEADRlrgEAA 414
PTZ00121 PTZ00121
MAEBL; Provisional
 163-277 1.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  163 QEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEmtKAREAKQERDAEALVKAAKQRKME-KLAAESDKKRILAQ 241
Cdd:PTZ00121  1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE--EKKKADELKKAEELKKAEEKKKAEeAKKAEEDKNMALRK 1582

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1845974384  242 IKADREAAQKKFG---KLVNTENASENTE-KKQETTVGKA 277
Cdd:PTZ00121  1583 AEEAKKAEEARIEevmKLYEEEKKMKAEEaKKAEEAKIKA 1622
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 163-244 1.40e-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: 40.67  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTK-AREAKQERDAEALVKAAKQRKMEKLAAEsdKKRILAQ 241
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqIEEREEQRAAEREEELEEGERLREEEAE--RRERIEE 333


                  ...
gi 1845974384 242 IKA 244
Cdd:pfam13868 334 ERQ 336
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 155-251 1.55e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 39.05  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 155 PIQSSSTSQEMTRELAEKV-ARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQ-RKMEKLAAE 232
Cdd:pfam16789   4 PLEQVLDIKKKRVEEAEKVvKDKKRALEKEKEKLAELEAERDKVRKHKKAKMQQLRDEMDRGTTSDKILQmKRYIKVVKE 83

                          90       100
                  ....*....|....*....|..
gi 1845974384 233 SDK---KRILAQIKADREAAQK 251
Cdd:pfam16789  84 RLKqeeKKVQDQKEQVRTAARN 105
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
167-252 1.79e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAE-KVARAKALLEQKKQkDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKR-------I 238
Cdd:COG2268   232 REIETaRIAEAEAELAKKKA-EERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREeaeleadV 310

                          90
                  ....*....|....
gi 1845974384 239 LAQIKADREAAQKK 252
Cdd:COG2268   311 RKPAEAEKQAAEAE 324
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 167-252 2.15e-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: 40.29  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKA-------LLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAA---ESDKK 236
Cdd:pfam13868   9 RELNSKLLAAKCnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqieEREQK 88

                          90
                  ....*....|....*.
gi 1845974384 237 RILAQIKADREAAQKK 252
Cdd:pfam13868  89 RQEEYEEKLQEREQMD 104
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 110-162 2.80e-03

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 39.44  E-value: 2.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1845974384 110 ATAQFVNGMPtaaANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTS 162
Cdd:PLN02983  146 PPAPVVMMQP---PPPHAMPPASPPAAQPAPSAPASSPPPTPASPPPAKAPKS 195
dnaK PRK00290
molecular chaperone DnaK; Provisional
 182-252 2.81e-03

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 40.08  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974384 182 QKKQKDAEKKREADKHVKEEMtkarEAKQErdAEALVKAAkqRKM-----EKLAAEsDKKRILAQIKADREAAQKK 252
Cdd:PRK00290  506 ERMVKDAEANAEEDKKRKELV----EARNQ--ADSLIYQT--EKTlkelgDKVPAD-EKEKIEAAIKELKEALKGE 572
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 127-251 3.10e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 127 STPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTS--------QEMTRELAEKVARAKA--LLEQKKQKDAEKKREADK 196
Cdd:TIGR02794  23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQkkpaakkeQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEK 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 197 HVK--EEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADREAAQK 251
Cdd:TIGR02794 103 AAKqaEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAK 159
PTZ00121 PTZ00121
MAEBL; Provisional
 162-252 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  162 SQEMTRELAEKVARaKALLEQKKQKDAeKKREADKHVKEEMTKaREAKQERDAEALVK--AAKQRKMEKLAAESDKKRIL 239
Cdd:PTZ00121  1655 AEEENKIKAAEEAK-KAEEDKKKAEEA-KKAEEDEKKAAEALK-KEAEEAKKAEELKKkeAEEKKKAEELKKAEEENKIK 1731

                           90
                   ....*....|...
gi 1845974384  240 AQiKADREAAQKK 252
Cdd:PTZ00121  1732 AE-EAKKEAEEDK 1743
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 163-252 5.13e-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: 39.13  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAA----------KQRKMEKLAAE 232
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILeylkekaereEEREAEREEIE 179

                          90       100
                  ....*....|....*....|
gi 1845974384 233 SDKKRILAQIKADREAAQKK 252
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDE 199
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
 129-252 5.17e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 37.92  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 129 PSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKvaRAKAL------LEQKKQKDAEKKREADKHVKEEM 202
Cdd:cd23703    15 KRPTRKDKTVEEYIAKTTPEPKKEPKPKSPLSEYQEWKRKMAEL--RRQNLreglreLEERKLKTEELRAKRSERKQAER 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1845974384 203 TKAREAKqERDAEAL----VKAAKQRKMEKLAAESDKKRILAQIKADREAAQKK 252
Cdd:cd23703    93 ERALNAP-EREDERLtlptIESALLGPLMRVRTDPEREERAAKRRANREAKELA 145
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 162-252 5.18e-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: 38.75  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 162 SQEMTRELAEKVA----RAKALLEQKKQKDAEKKREADK---HVKEEMTKAREAKQERDAEALvkaAKQRKMEKLAAESD 234
Cdd:pfam13868 190 RAQQEKAQDEKAErdelRAKLYQEEQERKERQKEREEAEkkaRQRQELQQAREEQIELKERRL---AEEAEREEEEFERM 266

                          90
                  ....*....|....*...
gi 1845974384 235 KKRILAQIKADREAAQKK 252
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKR 284
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 170-245 5.65e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 5.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974384 170 AEKV-ARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKAD 245
Cdd:cd06503    42 AEKAkEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKE 118
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 158-332 5.78e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 5.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  158 SSSTSQEMTRELAEKVARAkalLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKR 237
Cdd:PTZ00108  1122 KNTTPKDMWLEDLDKFEEA---LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNS 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384  238 ILAQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKAVPSDRCRLQVRLPDGSTFVEEFPSNDVlnSLVEIIRQKPS 317
Cdd:PTZ00108  1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDL--SKEGKPKNAPK 1276

                          170
                   ....*....|....*
gi 1845974384  318 IAGTTFEIQQPYPRR 332
Cdd:PTZ00108  1277 RVSAVQYSPPPPSKR 1291
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 163-277 5.89e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.16  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKD-----------AEKKREADKHVKEEMTKA---REAKQERDAEALVKAAKQRKMEK 228
Cdd:PRK05035  460 ARLEREKAAREARHKKAAEARAAKDkdavaaalarvKAKKAAATQPIVIKAGARpdnSAVIAAREARKAQARARQAEKQA 539

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1845974384 229 LAAESDKKrilAQIKADREAAQKKfgklvNTENASENTEKKQETTVGKA 277
Cdd:PRK05035  540 AAAADPKK---AAVAAAIARAKAK-----KAAQQAANAEAEEEVDPKKA 580
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
167-277 6.73e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEA---LVKAAKQRKMEKLAAESDKKRILAqiK 243
Cdd:COG3064    26 RAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAakkLAEAEKAAAEAEKKAAAEKAKAAK--E 103

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1845974384 244 ADREAAQKKFGKLVNTENASENTEKKQETTVGKA 277
Cdd:COG3064   104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKA 137
PRK12472 PRK12472
hypothetical protein; Provisional
 121-271 7.47e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 38.70  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 121 AAANQLSTPS-PSPAPvqvPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKAL------LEQ-KKQKDAEKKR 192
Cdd:PRK12472  167 AAPVDISHPAlFVPKA---EALAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAPLkaslrkLERaKARADAELKR 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 193 eADKHV---KEEMTKAR-EAKQERDAEALVKAAKQRKMEKLAAESdkKRILAQikADREAAQKKFGKLVNTENASENTEK 268
Cdd:PRK12472  244 -ADKALaaaKTDEAKARaEERQQKAAQQAAEAATQLDTAKADAEA--KRAAAA--ATKEAAKAAAAKKAETAKAATDAKL 318


                  ...
gi 1845974384 269 KQE 271
Cdd:PRK12472  319 ALE 321
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 104-250 8.11e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 38.78  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 104 RAKFDKATAQfvngmptaaanQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKALLEQK 183
Cdd:PRK05035  556 RAKAKKAAQQ-----------AANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARA 624

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974384 184 KQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKK-RILAQI---KAdREAAQ 250
Cdd:PRK05035  625 KAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKaAVAAAIaraKA-KKAAQ 694
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
153-274 8.18e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 38.42  E-value: 8.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 153 TAPIQSSSTSQEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAE 232
Cdd:PRK07735  150 TEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGD 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1845974384 233 S----DKKRILAQIKADREAAQKkfGKLVNTENASENTEKKQETTV 274
Cdd:PRK07735  230 SgdedAKAKAIAAAKAKAAAAAR--AKTKGAEGKKEEEPKQEEPSV 273
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 163-281 8.56e-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: 37.98  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 163 QEMTRELAEKVARAKALLEQKKQKDAEKKR-EAD-KHVKEEMTKARE----AKQERDAEALVK---AAKQRK-------- 225
Cdd:COG1579    34 AELEDELAALEARLEAAKTELEDLEKEIKRlELEiEEVEARIKKYEEqlgnVRNNKEYEALQKeieSLKRRIsdledeil 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845974384 226 --MEKL----AAESDKKRILAQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKAVPSD 281
Cdd:COG1579   114 elMERIeeleEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 103-251 8.88e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 38.69  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 103 FRAKFDKATAQFVNGMPTAAANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKALLEQ 182
Cdd:PRK07994  359 FHPAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA 438

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974384 183 KKQK--DAEKKREADKhVKEEMTKAREAKQERDAEALVKAAKQRKmeKLAAESDKKRILAQIKADREAAQK 251
Cdd:PRK07994  439 KKSEpaAASRARPVNS-ALERLASVRPAPSALEKAPAKKEAYRWK--ATNPVEVKKEPVATPKALKKALEH 506
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 167-270 8.99e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 38.39  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974384 167 RELAEKVARAK-------ALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERdAEALVKAAKQRKMEKLAAESDKKRIL 239
Cdd:PRK05035  442 EQEKKKAEEAKarfearqARLEREKAAREARHKKAAEARAAKDKDAVAAALAR-VKAKKAAATQPIVIKAGARPDNSAVI 520

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974384 240 AQIKADREAAQKkfgKLVNTENASENTEKKQ 270
Cdd:PRK05035  521 AAREARKAQARA---RQAEKQAAAAADPKKA 548
 
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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