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Conserved domains on  [gi|489178376|ref|WP_003087885|]
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MULTISPECIES: SPFH domain-containing protein [Pseudomonas]

Protein Classification

SPFH domain-containing protein( domain architecture ID 1004687)

uncharacterized SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  17766116|10542406
SCOP:  4003722

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
94-287 1.49e-08

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


The actual alignment was detected with superfamily member pfam01145:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 177  Bit Score: 54.25  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376   94 TIEAFPIVFLGNVDAKVESSARFRLPGGEPFlKMAQEYRNPDNfIRTALVPAIKETLQATASLMSADDYYaGARSEFAAE 173
Cdd:pfam01145  46 EVSVQTVLTKDGVPVNVDVTVIYRVNPDDPP-KLVQNVFGSDD-LQELLRRVLESALREIIARYTLEELL-SNREELAEE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  174 FENQLndglylikrkevrgprgaiphqtailqagteqgafgdnnasqfvtekvtdakgipvrkQQQFRKFGVEVVEARIT 253
Cdd:pfam01145 123 IKNAL----------------------------------------------------------QEELAKYGVEIIDVQIT 144
                         170       180       190
                  ....*....|....*....|....*....|....
gi 489178376  254 NVDPNPQYKQRMVKVQQALAElAVARQNRLKEEE 287
Cdd:pfam01145 145 DIDPPPEIAEAIEAKQTAEQE-AEAEIARAEAEA 177
YqiK super family cl34451
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
267-440 2.56e-05

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


The actual alignment was detected with superfamily member COG2268:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 267 KVQQALAELAVARQNRLKEEEEKllvTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQRAE-----IEKQ 341
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETA---RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEleadvRKPA 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 342 TAELLRDKATVTAQATKITAD--AEAYAREAVIKADGALQP--KLDALIAINKVWAEAAAQAP--VPSVMM---GAGANG 412
Cdd:COG2268  315 EAEKQAAEAEAEAEAEAIRAKglAEAEGKRALAEAWNKLGDaaILLMLIEKLPEIAEAAAKPLekIDKITIidgGNGGNG 394
                        170       180
                 ....*....|....*....|....*....
gi 489178376 413 AASRQ-DEIGQLMGVLATKAARDLALDLK 440
Cdd:COG2268  395 AGSAVaEALAPLLESLLEETGLDLPGLLK 423
 
Name Accession Description Interval E-value
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
94-287 1.49e-08

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 54.25  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376   94 TIEAFPIVFLGNVDAKVESSARFRLPGGEPFlKMAQEYRNPDNfIRTALVPAIKETLQATASLMSADDYYaGARSEFAAE 173
Cdd:pfam01145  46 EVSVQTVLTKDGVPVNVDVTVIYRVNPDDPP-KLVQNVFGSDD-LQELLRRVLESALREIIARYTLEELL-SNREELAEE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  174 FENQLndglylikrkevrgprgaiphqtailqagteqgafgdnnasqfvtekvtdakgipvrkQQQFRKFGVEVVEARIT 253
Cdd:pfam01145 123 IKNAL----------------------------------------------------------QEELAKYGVEIIDVQIT 144
                         170       180       190
                  ....*....|....*....|....*....|....
gi 489178376  254 NVDPNPQYKQRMVKVQQALAElAVARQNRLKEEE 287
Cdd:pfam01145 145 DIDPPPEIAEAIEAKQTAEQE-AEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
237-338 3.53e-08

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 54.46  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 237 QQQFRKFGVEVVEARITNVDPNPQYKQRMVKVQQALAElAVARQNRLKEEEEKLLVTARGEKEVeakrqetlrdqieRTT 316
Cdd:COG0330  145 QEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE-REAAILEAEGYREAAIIRAEGEAQR-------------AII 210
                         90       100
                 ....*....|....*....|..
gi 489178376 317 QAETDKQLAVINAEREKQRAEI 338
Cdd:COG0330  211 EAEAYREAQILRAEGEAEAFRI 232
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
267-440 2.56e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 267 KVQQALAELAVARQNRLKEEEEKllvTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQRAE-----IEKQ 341
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETA---RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEleadvRKPA 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 342 TAELLRDKATVTAQATKITAD--AEAYAREAVIKADGALQP--KLDALIAINKVWAEAAAQAP--VPSVMM---GAGANG 412
Cdd:COG2268  315 EAEKQAAEAEAEAEAEAIRAKglAEAEGKRALAEAWNKLGDaaILLMLIEKLPEIAEAAAKPLekIDKITIidgGNGGNG 394
                        170       180
                 ....*....|....*....|....*....
gi 489178376 413 AASRQ-DEIGQLMGVLATKAARDLALDLK 440
Cdd:COG2268  395 AGSAVaEALAPLLESLLEETGLDLPGLLK 423
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
262-399 2.75e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.95  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 262 KQRMVKVQQALAEL---AVARQNRLKEEEEKLLVTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQRAEI 338
Cdd:PRK09510  79 EQRKKKEQQQAEELqqkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAA 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489178376 339 EKQTAELLRDKATVTAQATKITADAEAYAR-EAVIKADGALQPKLDALiAINKVWAEAAAQA 399
Cdd:PRK09510 159 AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEAE-AKKKAAAEAKKKA 219
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
256-384 2.80e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 46.75  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  256 DPNPQYKQRMVKVQQALA--ELAVARQNRLKEEEEKLLVTARGEKEveaKRQETLRDQIERTTQAETDKQLAVINAereK 333
Cdd:NF012221 1675 DAKQRHVDNQQKVKDAVAksEAGVAQGEQNQANAEQDIDDAKADAE---KRKDDALAKQNEAQQAESDANAAANDA---Q 1748
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489178376  334 QRAEIEKQTAELLRDKATVTAQATKITAD--------------AEAYAREAVIKADGALQPKLDA 384
Cdd:NF012221 1749 SRGEQDASAAENKANQAQADAKGAKQDESdkpnrqgaagsglsGKAYSVEGVAEPGSHINPDSPA 1813
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
224-356 6.89e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  224 EKVTDAKGIPVRKQQQFRKFGVEVVEARitNVDPNPQYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTARgEKEVEAK 303
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER-AREMERV 451
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489178376  304 RQETL--RDQIERTTQAETDKQLAVINAEREKQ-RAEIEKQTAELLRDKATVTAQA 356
Cdd:pfam17380 452 RLEEQerQQQVERLRQQEEERKRKKLELEKEKRdRKRAEEQRRKILEKELEERKQA 507
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
279-370 8.11e-04

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 41.13  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 279 RQN--RLKEEEEKLLVTARGEKEVEakrqetlrdqiertTQAETDKQLAVINAEREKQRAEIEKQtaELLRDKATVTAQA 356
Cdd:cd03406  165 RRNyeAMEAEKTKLLIAEQHQKVVE--------------KEAETERKRAVIEAEKDAEVAKIQMQ--QKIMEKEAEKKIS 228
                         90       100
                 ....*....|....*....|....*.
gi 489178376 357 T----------KITADAEAYA--REA 370
Cdd:cd03406  229 EiedemhlareKARADAEYYRalREA 254
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
243-304 7.02e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 38.33  E-value: 7.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489178376 243 FGVEVVEARITNVDPNPQYKQRMVKVQQAlAELAVARQNrlKEEEEKLLVTARGEKEVEAKR 304
Cdd:cd03407  130 YGYEIVKTLVTDIEPDASVKAAMNEINAA-QRLREAAEE--KAEAEKILQVKAAEAEAEAKR 188
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
260-360 9.69e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 9.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376   260 QYKQRMVKVQQALAELAvARQNRLKEE---EEKLLVTARGEKEVEAKRQETLRDQIE--RTTQAETDKQLAVINAEREKQ 334
Cdd:TIGR02168  327 ELESKLDELAEELAELE-EKLEELKEElesLEAELEELEAELEELESRLEELEEQLEtlRSKVAQLELQIASLNNEIERL 405
                           90       100
                   ....*....|....*....|....*.
gi 489178376   335 RAEIEKQTAELLRDKATVTAQATKIT 360
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLE 431
 
Name Accession Description Interval E-value
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
94-287 1.49e-08

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 54.25  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376   94 TIEAFPIVFLGNVDAKVESSARFRLPGGEPFlKMAQEYRNPDNfIRTALVPAIKETLQATASLMSADDYYaGARSEFAAE 173
Cdd:pfam01145  46 EVSVQTVLTKDGVPVNVDVTVIYRVNPDDPP-KLVQNVFGSDD-LQELLRRVLESALREIIARYTLEELL-SNREELAEE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  174 FENQLndglylikrkevrgprgaiphqtailqagteqgafgdnnasqfvtekvtdakgipvrkQQQFRKFGVEVVEARIT 253
Cdd:pfam01145 123 IKNAL----------------------------------------------------------QEELAKYGVEIIDVQIT 144
                         170       180       190
                  ....*....|....*....|....*....|....
gi 489178376  254 NVDPNPQYKQRMVKVQQALAElAVARQNRLKEEE 287
Cdd:pfam01145 145 DIDPPPEIAEAIEAKQTAEQE-AEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
237-338 3.53e-08

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 54.46  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 237 QQQFRKFGVEVVEARITNVDPNPQYKQRMVKVQQALAElAVARQNRLKEEEEKLLVTARGEKEVeakrqetlrdqieRTT 316
Cdd:COG0330  145 QEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE-REAAILEAEGYREAAIIRAEGEAQR-------------AII 210
                         90       100
                 ....*....|....*....|..
gi 489178376 317 QAETDKQLAVINAEREKQRAEI 338
Cdd:COG0330  211 EAEAYREAQILRAEGEAEAFRI 232
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
267-440 2.56e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.40  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 267 KVQQALAELAVARQNRLKEEEEKllvTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQRAE-----IEKQ 341
Cdd:COG2268  238 RIAEAEAELAKKKAEERREAETA---RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAEleadvRKPA 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 342 TAELLRDKATVTAQATKITAD--AEAYAREAVIKADGALQP--KLDALIAINKVWAEAAAQAP--VPSVMM---GAGANG 412
Cdd:COG2268  315 EAEKQAAEAEAEAEAEAIRAKglAEAEGKRALAEAWNKLGDaaILLMLIEKLPEIAEAAAKPLekIDKITIidgGNGGNG 394
                        170       180
                 ....*....|....*....|....*....
gi 489178376 413 AASRQ-DEIGQLMGVLATKAARDLALDLK 440
Cdd:COG2268  395 AGSAVaEALAPLLESLLEETGLDLPGLLK 423
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
262-399 2.75e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.95  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 262 KQRMVKVQQALAEL---AVARQNRLKEEEEKLLVTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQRAEI 338
Cdd:PRK09510  79 EQRKKKEQQQAEELqqkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAA 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489178376 339 EKQTAELLRDKATVTAQATKITADAEAYAR-EAVIKADGALQPKLDALiAINKVWAEAAAQA 399
Cdd:PRK09510 159 AAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEAE-AKKKAAAEAKKKA 219
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
256-384 2.80e-05

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 46.75  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  256 DPNPQYKQRMVKVQQALA--ELAVARQNRLKEEEEKLLVTARGEKEveaKRQETLRDQIERTTQAETDKQLAVINAereK 333
Cdd:NF012221 1675 DAKQRHVDNQQKVKDAVAksEAGVAQGEQNQANAEQDIDDAKADAE---KRKDDALAKQNEAQQAESDANAAANDA---Q 1748
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489178376  334 QRAEIEKQTAELLRDKATVTAQATKITAD--------------AEAYAREAVIKADGALQPKLDA 384
Cdd:NF012221 1749 SRGEQDASAAENKANQAQADAKGAKQDESdkpnrqgaagsglsGKAYSVEGVAEPGSHINPDSPA 1813
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
224-356 6.89e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 6.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  224 EKVTDAKGIPVRKQQQFRKFGVEVVEARitNVDPNPQYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTARgEKEVEAK 303
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER-AREMERV 451
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489178376  304 RQETL--RDQIERTTQAETDKQLAVINAEREKQ-RAEIEKQTAELLRDKATVTAQA 356
Cdd:pfam17380 452 RLEEQerQQQVERLRQQEEERKRKKLELEKEKRdRKRAEEQRRKILEKELEERKQA 507
PTZ00121 PTZ00121
MAEBL; Provisional
224-370 3.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  224 EKVTDAKGIPVRKQQQFRKfgveVVEARITNVDPNPQYKQRMVKVQQALAELAVARQNRL-KEEEEKLLVTARGEKEVEA 302
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKK----AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEE 1645
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489178376  303 KRQEtlrdqiERTTQAETDKQlavINAEREKQRAEIEKQTAELLRDKATVTAQAtkitadAEAYAREA 370
Cdd:PTZ00121 1646 KKKA------EELKKAEEENK---IKAAEEAKKAEEDKKKAEEAKKAEEDEKKA------AEALKKEA 1698
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
266-367 3.81e-04

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 266 VKVQQALAELAVARQNRLKEEEEKLLVTARGEKEVEA---------KRQETLRDQI-ERTTQAET-DKQLAVINAEREKQ 334
Cdd:COG1579   57 LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkeieslkRRISDLEDEIlELMERIEElEEELAELEAELAEL 136
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489178376 335 RAEIEKQTAELLRDKATVTAQATKITADAEAYA 367
Cdd:COG1579  137 EAELEEKKAELDEELAELEAELEELEAEREELA 169
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
263-428 3.83e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 263 QRMVKVQQALAELAVARQNRLKEEEEKLLVTARGEKEVEAKRQETLrdqierTTQAETDKQLAVINAEREKQRAEIEKQT 342
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAA------AKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 343 AELLRDKATVTAQATKITADAEAYAREAVIKADGALQPKLDALIAINKVWAEAAAQAPvpsvmmGAGANGAASRQDEIGQ 422
Cdd:PRK09510 188 EAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAK------AAEKAAAAKAAAEVDD 261

                 ....*.
gi 489178376 423 LMGVLA 428
Cdd:PRK09510 262 LFGGLD 267
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
260-399 5.83e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 260 QYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTARGEKEVEAKRQEtLRDQIERTTQAETD--------KQLAVINAER 331
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDiarleerrRELEERLEEL 321
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489178376 332 EKQRAEIEKQTAELLRDKATVTAQATKITADAEAyAREAVIKADGALQPKLDALIAINKVWAEAAAQA 399
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
258-382 7.77e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 258 NPQYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTARGEKEVEAKRQE------TLRDQIERTTQAETDKQLAVinAER 331
Cdd:COG4942  127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEleallaELEEERAALEALKAERQKLL--ARL 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489178376 332 EKQRAEIEKQTAELLRDKATVTAQATKITADAEAYAREAVIKADGALQPKL 382
Cdd:COG4942  205 EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
269-399 7.88e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 269 QQALAELAVARQNRLKEEEEKLLVTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAEREKQ-----RAEIEKQTA 343
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerRRELEERLE 319
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489178376 344 ELLRDKATVTAQATKITADAEAyAREAVIKADGALQPKLDALIAINKVWAEAAAQA 399
Cdd:COG1196  320 ELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
279-370 8.11e-04

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 41.13  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 279 RQN--RLKEEEEKLLVTARGEKEVEakrqetlrdqiertTQAETDKQLAVINAEREKQRAEIEKQtaELLRDKATVTAQA 356
Cdd:cd03406  165 RRNyeAMEAEKTKLLIAEQHQKVVE--------------KEAETERKRAVIEAEKDAEVAKIQMQ--QKIMEKEAEKKIS 228
                         90       100
                 ....*....|....*....|....*.
gi 489178376 357 T----------KITADAEAYA--REA 370
Cdd:cd03406  229 EiedemhlareKARADAEYYRalREA 254
PRK14147 PRK14147
heat shock protein GrpE; Provisional
317-402 1.63e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237625 [Multi-domain]  Cd Length: 172  Bit Score: 39.16  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 317 QAETDKqlavINAEREKQRAEIEKQTAELLRDKATVTAQATKITADAEAYAREAVIKADGALQPKLDALIAinkvWAEAA 396
Cdd:PRK14147  17 PPETDP----LKAEVESLRSEIALVKADALRERADLENQRKRIARDVEQARKFANEKLLGELLPVFDSLDA----GLTAA 88

                 ....*.
gi 489178376 397 AQAPVP 402
Cdd:PRK14147  89 GTEPSP 94
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
246-399 1.93e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.37  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  246 EVVEARITNVDPNPQYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTA--------RGEKEVEAKRQETLRDQIE---- 313
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDAdkaqqkadFAQDNADKQRDEVRQKQQEaknl 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  314 ----RTTQAETDKQLAVINA-EREKQRAEIEKQTAELLRDKatvTAQATKITADAEAYAREAVIKADGALQPKLDALIAI 388
Cdd:pfam05262 261 pkpaDTSSPKEDKQVAENQKrEIEKAQIEIKKNDEEALKAK---DHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL 337
                         170
                  ....*....|.
gi 489178376  389 NKVWAEAAAQA 399
Cdd:pfam05262 338 QKTKPQVEAQP 348
PTZ00121 PTZ00121
MAEBL; Provisional
230-377 2.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  230 KGIPVRKQQQFRKfGVEVVEARITNVDPNPQYKQRMVKVQQALAELAVARQNRLKEEEEKLLVTARGEKEvEAKRQETLR 309
Cdd:PTZ00121 1386 KAEEKKKADEAKK-KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAK 1463
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  310 DQIERTTQAETDKQLA--VINAEREKQRAEIEKQTAELLRDKATVTAQATKITADAEAYAREAVIKADGA 377
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAeeAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
260-399 3.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 260 QYKQRMVKVQQALAELAVARQNRLKEEEE-------KLLVTARGEKEVEAKRQETLRDQIERTTQAETDKQLAVINAERE 332
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELEleeaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489178376 333 KQRAEIEKQTAELLRDKATVTAQATKITADAEAYAREAvikadGALQPKLDALIAINKVWAEAAAQA 399
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-----AELAEAEEELEELAEELLEALRAA 395
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
303-379 5.57e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.09  E-value: 5.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489178376 303 KRQETLRDQIERTTQAETDKQLAVINAEREKQRAEIEKQTAELLRDKATVTAQATKITADAEAYAREAVIKADGALQ 379
Cdd:COG2268  193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
267-437 6.84e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 267 KVQQALAELAVArQNRLKEEEEKLLVTARGEKEVEAKRQETLRDQIERTTQAETDKQLAvinAEREKQRAEIEKQTAELL 346
Cdd:COG1196  338 ELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA---AELAAQLEELEEAEEALL 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376 347 RDKATVTAQAtkitADAEAYAREAVIKADGALQPKLDALIAINKVWAEAAAQApvpsVMMGAGANGAASRQDEIGQLMGV 426
Cdd:COG1196  414 ERLERLEEEL----EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL----ELLAELLEEAALLEAALAELLEE 485
                        170
                 ....*....|.
gi 489178376 427 LATKAARDLAL 437
Cdd:COG1196  486 LAEAAARLLLL 496
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
243-304 7.02e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 38.33  E-value: 7.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489178376 243 FGVEVVEARITNVDPNPQYKQRMVKVQQAlAELAVARQNrlKEEEEKLLVTARGEKEVEAKR 304
Cdd:cd03407  130 YGYEIVKTLVTDIEPDASVKAAMNEINAA-QRLREAAEE--KAEAEKILQVKAAEAEAEAKR 188
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
237-280 7.32e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259800  Cd Length: 231  Bit Score: 37.92  E-value: 7.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489178376 237 QQQFRKFGVEVVEARITNVDPNPQYKQRMVKVQQALAELAvARQ 280
Cdd:cd03402  140 QERLAVAGVEVIEARITHLAYAPEIAQAMLQRQQASAIIA-ARQ 182
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
260-360 9.69e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 9.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376   260 QYKQRMVKVQQALAELAvARQNRLKEE---EEKLLVTARGEKEVEAKRQETLRDQIE--RTTQAETDKQLAVINAEREKQ 334
Cdd:TIGR02168  327 ELESKLDELAEELAELE-EKLEELKEElesLEAELEELEAELEELESRLEELEEQLEtlRSKVAQLELQIASLNNEIERL 405
                           90       100
                   ....*....|....*....|....*.
gi 489178376   335 RAEIEKQTAELLRDKATVTAQATKIT 360
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLE 431
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
259-422 9.92e-03

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 38.12  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  259 PQYKQRMVKVQQALAELAVARQNrlkEEEEKllVTARGEKEVEAKRQETlrDQIERTTQAETDKQLAV----INAEREKQ 334
Cdd:pfam04747  64 PQQVEKVKKSEKKKAQKQIAKDH---EAEQK--VNAKKAAEKEARRAEA--EAKKRAAQEEEHKQWKAeqerIQKEQEKK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489178376  335 RAEIEKQTAELLRDKATVTAQATKITADAEAYAREAVikadgalqpklDALIAINKVWAE-AAAQAPVPSVMMGAGANGA 413
Cdd:pfam04747 137 EADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPV-----------EEEIVVKKVANDrSAAPAPEPKTPTNTPAEPA 205

                  ....*....
gi 489178376  414 ASRQDEIGQ 422
Cdd:pfam04747 206 EQVQEITGK 214
 
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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