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Conserved domains on  [gi|939220313|gb|EDV37397|]
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uncharacterized protein Dana_GF13426, isoform F [Drosophila ananassae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqiK super family cl34451
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1068-1180 1.31e-08

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: 59.12  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1068 EKQSRQAEIEKQTRLAEIEkQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELEtqsrlAELEKRAAAED 1147
Cdd:COG2268   245 ELAKKKAEERREAETARAE-AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE-----ADVRKPAEAEK 318

                          90       100       110
                  ....*....|....*....|....*....|...
gi 939220313 1148 QQKREifnRNSAEDQQKREifisiETEANAQGR 1180
Cdd:COG2268   319 QAAEA---EAEAEAEAIRA-----KGLAEAEGK 343
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 263-287 9.65e-07

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


:

Pssm-ID: 464037  Cd Length: 25  Bit Score: 46.42  E-value: 9.65e-07
                           10        20
                   ....*....|....*....|....*
gi 939220313   263 DLTPCPCCSRTFNVNALRKHIVICE 287
Cdd:pfam13913    1 ELVPCPICGRTFNPDRLAKHEKICK 25
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 425-446 5.80e-04

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


:

Pssm-ID: 464037  Cd Length: 25  Bit Score: 38.33  E-value: 5.80e-04
                           10        20
                   ....*....|....*....|..
gi 939220313   425 RCPHCDRTFNPKAFDRHVEWCK 446
Cdd:pfam13913    4 PCPICGRTFNPDRLAKHEKICK 25
zinc_ribbon_2 pfam13240
zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as ...
 1523-1543 2.58e-03

zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR. pfam12773.


:

Pssm-ID: 433054 [Multi-domain]  Cd Length: 21  Bit Score: 36.71  E-value: 2.58e-03
                           10        20
                   ....*....|....*....|.
gi 939220313  1523 FCHECGAKfIVEQAKFCMECG 1543
Cdd:pfam13240    1 FCPNCGAE-NPDGAKFCPKCG 20
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1061-1299 7.41e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1061 DVSSQHEEKQSRQAEI-EKQTRLAEIEKqnRLAEIEKqsrlaEIEKQSRLAELEMQTRLAEMEKQnrLAELETQSRLAEL 1139
Cdd:TIGR02169  245 QLASLEEELEKLTEEIsELEKRLEEIEQ--LLEELNK-----KIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1140 EKRAAAEDQQKreIFNRNSAEDQQKREIFISIETEAnaqgrspISPDSLRHMVGNSQTPIDVLHIENGNEPEHAR--FSK 1217
Cdd:TIGR02169  316 ELEDAEERLAK--LEAEIDKLLAEIEELEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAetRDE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1218 ISDTEDAGEEPGDRPSQLNSN------RLVQSSSSCALAPNvQLNNAKNLIQKMQSDFRQLGEEASASMRRTLIANSGRS 1291
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKREldrlqeELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465


                   ....*...
gi 939220313  1292 EEQQQMRD 1299
Cdd:TIGR02169  466 KYEQELYD 473
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1068-1180 1.31e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 59.12  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1068 EKQSRQAEIEKQTRLAEIEkQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELEtqsrlAELEKRAAAED 1147
Cdd:COG2268   245 ELAKKKAEERREAETARAE-AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE-----ADVRKPAEAEK 318

                          90       100       110
                  ....*....|....*....|....*....|...
gi 939220313 1148 QQKREifnRNSAEDQQKREifisiETEANAQGR 1180
Cdd:COG2268   319 QAAEA---EAEAEAEAIRA-----KGLAEAEGK 343
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 263-287 9.65e-07

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464037  Cd Length: 25  Bit Score: 46.42  E-value: 9.65e-07
                           10        20
                   ....*....|....*....|....*
gi 939220313   263 DLTPCPCCSRTFNVNALRKHIVICE 287
Cdd:pfam13913    1 ELVPCPICGRTFNPDRLAKHEKICK 25
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 1062-1142 8.27e-06

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: 49.60  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1062 VSSQHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEmEKQNRLAELETQSRLAELEK 1141
Cdd:cd03406   180 IAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAR-EKARADAEYYRALREAEANK 258


                  .
gi 939220313 1142 R 1142
Cdd:cd03406   259 L 259
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1065-1178 1.29e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.42  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEieKQTRLAEIEKQnRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELETQSRLAELEKRAA 1144
Cdd:PRK09510   88 QAEELQQKQAA--EQERLKQLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 939220313 1145 AEDQQKREifnrnsAEDQQKREIFISIETEANAQ 1178
Cdd:PRK09510  165 AEAKKKAE------AEAAKKAAAEAKKKAEAEAA 192
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1069-1174 1.44e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.88  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1069 KQSR-QAEIEKQTRLaEIEKQNRLAEIEKQSRLAEiEKQSRLAE---LEMQTRLAEMEKQNRLAELETQSRLAELEKRAA 1144
Cdd:pfam05672   21 RQAReQREREEQERL-EKEEEERLRKEELRRRAEE-ERARREEEarrLEEERRREEEERQRKAEEEAEEREQREQEEQER 98

                           90       100       110
                   ....*....|....*....|....*....|...
gi 939220313  1145 AEDQQKR-EIFNRNSAEDQ-QKRE-IFISIETE 1174
Cdd:pfam05672   99 LQKQKEEaEAKAREEAERQrQEREkIMQQEEQE 131
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 425-446 5.80e-04

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464037  Cd Length: 25  Bit Score: 38.33  E-value: 5.80e-04
                           10        20
                   ....*....|....*....|..
gi 939220313   425 RCPHCDRTFNPKAFDRHVEWCK 446
Cdd:pfam13913    4 PCPICGRTFNPDRLAKHEKICK 25
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1068-1177 2.54e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1068 EKQSRQAEIEKQTRLAEIEKQN-RLAEIE-----KQSRLAEIEKQSRLAE----------------LEMQTRLAEMEKQN 1125
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRkRLSELKakleaLEEELSEIEDPKGEDEeipeeelsledvqaelQRVEEEIRALEPVN 974

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 939220313  1126 RLAELE---TQSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANA 1177
Cdd:TIGR02169  975 MLAIQEyeeVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINE 1029
zinc_ribbon_2 pfam13240
zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as ...
 1523-1543 2.58e-03

zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR. pfam12773.


Pssm-ID: 433054 [Multi-domain]  Cd Length: 21  Bit Score: 36.71  E-value: 2.58e-03
                           10        20
                   ....*....|....*....|.
gi 939220313  1523 FCHECGAKfIVEQAKFCMECG 1543
Cdd:pfam13240    1 FCPNCGAE-NPDGAKFCPKCG 20
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1061-1299 7.41e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1061 DVSSQHEEKQSRQAEI-EKQTRLAEIEKqnRLAEIEKqsrlaEIEKQSRLAELEMQTRLAEMEKQnrLAELETQSRLAEL 1139
Cdd:TIGR02169  245 QLASLEEELEKLTEEIsELEKRLEEIEQ--LLEELNK-----KIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1140 EKRAAAEDQQKreIFNRNSAEDQQKREIFISIETEAnaqgrspISPDSLRHMVGNSQTPIDVLHIENGNEPEHAR--FSK 1217
Cdd:TIGR02169  316 ELEDAEERLAK--LEAEIDKLLAEIEELEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAetRDE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1218 ISDTEDAGEEPGDRPSQLNSN------RLVQSSSSCALAPNvQLNNAKNLIQKMQSDFRQLGEEASASMRRTLIANSGRS 1291
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKREldrlqeELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465


                   ....*...
gi 939220313  1292 EEQQQMRD 1299
Cdd:TIGR02169  466 KYEQELYD 473
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1068-1180 1.31e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 59.12  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1068 EKQSRQAEIEKQTRLAEIEkQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELEtqsrlAELEKRAAAED 1147
Cdd:COG2268   245 ELAKKKAEERREAETARAE-AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE-----ADVRKPAEAEK 318

                          90       100       110
                  ....*....|....*....|....*....|...
gi 939220313 1148 QQKREifnRNSAEDQQKREifisiETEANAQGR 1180
Cdd:COG2268   319 QAAEA---EAEAEAEAIRA-----KGLAEAEGK 343
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 263-287 9.65e-07

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464037  Cd Length: 25  Bit Score: 46.42  E-value: 9.65e-07
                           10        20
                   ....*....|....*....|....*
gi 939220313   263 DLTPCPCCSRTFNVNALRKHIVICE 287
Cdd:pfam13913    1 ELVPCPICGRTFNPDRLAKHEKICK 25
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1067-1160 3.00e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.41  E-value: 3.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1067 EEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRL-AEMEKQN--RLAELETQSRLAELEKRA 1143
Cdd:COG2268   261 RAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKpAEAEKQAaeAEAEAEAEAIRAKGLAEA 340

                          90
                  ....*....|....*..
gi 939220313 1144 AAEdQQKREIFNRNSAE 1160
Cdd:COG2268   341 EGK-RALAEAWNKLGDA 356
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 1062-1142 8.27e-06

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: 49.60  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1062 VSSQHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEmEKQNRLAELETQSRLAELEK 1141
Cdd:cd03406   180 IAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAR-EKARADAEYYRALREAEANK 258


                  .
gi 939220313 1142 R 1142
Cdd:cd03406   259 L 259
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1062-1180 9.23e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 9.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1062 VSSQHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQsrLAELEmqTRLAEMEKQNRLAELETQSRLAELEK 1141
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE--LEELE--EELEEAEEELEEAEAELAEAEEALLE 369

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 939220313 1142 RAAAEDQQKREIFNRNSAEDQQKREIFISIETEANAQGR 1180
Cdd:COG1196   370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 1075-1146 1.22e-05

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: 48.83  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939220313 1075 EIEKQTRLAEIEKQN---RLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELETQSRLAELEKRAAAE 1146
Cdd:cd03406   172 EAEKTKLLIAEQHQKvveKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREKARADAE 246
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1065-1178 1.27e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEKQTRLAEIEKQ---NRLAEIEKQS---RLAEIEKQSRLAELEMQ-TRLAEMEKQNRLAELETQSRLA 1137
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEelrLELEELELELeeaQAEEYELLAELARLEQDiARLEERRRELEERLEELEEELA 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 939220313 1138 ELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANAQ 1178
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1065-1178 1.29e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.42  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEieKQTRLAEIEKQnRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELETQSRLAELEKRAA 1144
Cdd:PRK09510   88 QAEELQQKQAA--EQERLKQLEKE-RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA 164

                          90       100       110
                  ....*....|....*....|....*....|....
gi 939220313 1145 AEDQQKREifnrnsAEDQQKREIFISIETEANAQ 1178
Cdd:PRK09510  165 AEAKKKAE------AEAAKKAAAEAKKKAEAEAA 192
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1065-1180 2.24e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEKQTRLAEIEKQNRlAEIEKQSRLAEIEKQsrLAELEMQTRLAEMEKQNRLAELETQSRlaELEKRAA 1144
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEE-ELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEE 379

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 939220313 1145 AEDQQKREIFNRNSAEDQQKREIFISIETEANAQGR 1180
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1068-1180 3.76e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1068 EKQSRQAEIEKQTRLAEiEKQNRLAEIEKQSRLAEIEKQSRLAELEmqTRLAEMEKQNRLAELETQSRLAELEKRAAAED 1147
Cdd:COG1196   292 ELLAELARLEQDIARLE-ERRRELEERLEELEEELAELEEELEELE--EELEELEEELEEAEEELEEAEAELAEAEEALL 368

                          90       100       110
                  ....*....|....*....|....*....|...
gi 939220313 1148 QQKREIFNRNSAEDQQKREIFISIETEANAQGR 1180
Cdd:COG1196   369 EAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1065-1180 5.75e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.49  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQsrlaelemqtRLAEMEKQNRLAEletQSRLAELEKRAA 1144
Cdd:PRK09510   68 QQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE----------RLAAQEQKKQAEE---AAKQAALKQKQA 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 939220313 1145 AEDQQKREIFNRNSAEDQQKREIFISIETEANAQGR 1180
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1066-1178 8.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1066 HEEKQSRQAEIEK-QTRLAEIEKQnrLAEIEKQsrLAEIEKQSRLAELEMQTRLA-EMEKQNRLAELE-----TQSRLAE 1138
Cdd:COG1196   238 EAELEELEAELEElEAELEELEAE--LAELEAE--LEELRLELEELELELEEAQAeEYELLAELARLEqdiarLEERRRE 313

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 939220313 1139 LEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANAQ 1178
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1064-1180 9.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 9.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1064 SQHEEKQSRQAEIEKQ---TRLAEIEKQNRLAEIEKQSRLAE---IEKQSRLAELEMQTRLAEMEKQNRLAELET-QSRL 1136
Cdd:COG1196   267 AELEELRLELEELELEleeAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEELEElEEEL 346

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 939220313 1137 AELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANAQGR 1180
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1069-1174 1.44e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.88  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1069 KQSR-QAEIEKQTRLaEIEKQNRLAEIEKQSRLAEiEKQSRLAE---LEMQTRLAEMEKQNRLAELETQSRLAELEKRAA 1144
Cdd:pfam05672   21 RQAReQREREEQERL-EKEEEERLRKEELRRRAEE-ERARREEEarrLEEERRREEEERQRKAEEEAEEREQREQEEQER 98

                           90       100       110
                   ....*....|....*....|....*....|...
gi 939220313  1145 AEDQQKR-EIFNRNSAEDQ-QKRE-IFISIETE 1174
Cdd:pfam05672   99 LQKQKEEaEAKAREEAERQrQEREkIMQQEEQE 131
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1068-1167 4.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1068 EKQSRQAEIEKQTRLAEiEKQNRLAEIEKQSRLAEIEKQSRLAELEmQTRLAEMEKQNRLAELEtqSRLAELEKRAAAED 1147
Cdd:COG1196   233 KLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEYELL--AELARLEQDIARLE 308

                          90       100
                  ....*....|....*....|
gi 939220313 1148 QQKREIFNRNSAEDQQKREI 1167
Cdd:COG1196   309 ERRRELEERLEELEEELAEL 328
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1065-1163 4.12e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEKQ---TRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEM---QTRLAEMEKqnRLAEL-ETQSRLA 1137
Cdd:COG4717    89 EYAELQEELEELEEEleeLEAELEELREELEKLEKLLQLLPLYQELEALEAELaelPERLEELEE--RLEELrELEEELE 166

                          90       100
                  ....*....|....*....|....*.
gi 939220313 1138 ELEKRAAAEDQQKREIFNRNSAEDQQ 1163
Cdd:COG4717   167 ELEAELAELQEELEELLEQLSLATEE 192
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1072-1178 5.24e-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: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1072 RQAEIEKQTRLAeIEKQNRLAEIEKQSRLAEI----------EKQSRLAELEMQTRLA--------EMEKQNRLAELETQ 1133
Cdd:COG2268   204 AEAEAERETEIA-IAQANREAEEAELEQEREIetariaeaeaELAKKKAEERREAETAraeaeaayEIAEANAEREVQRQ 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 939220313 1134 SRLAELEKRAAAedQQKReifnRNSAEDQQKREIFISIETEANAQ 1178
Cdd:COG2268   283 LEIAEREREIEL--QEKE----AEREEAELEADVRKPAEAEKQAA 321
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1067-1178 5.61e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1067 EEKQSRQAEIEKQTRLAEIEKQNRL-----------AEIEKQSRL--------------AEIEKQSRLAELEMQTRLAEM 1121
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAaaeaeqkakeeAEEERLAELeakrqaeeeareakAEAEQRAAELAAEAAKKLAEA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 939220313 1122 EKQNRLAELETQSRLAELEKRAAAEDQQKREIFN-RNSAEDQQKREifisIETEANAQ 1178
Cdd:COG3064    83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAaEKEKAEEAKRK----AEEEAKRK 136
zf-C2HC_2 pfam13913
zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.
 425-446 5.80e-04

zinc-finger of a C2HC-type; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464037  Cd Length: 25  Bit Score: 38.33  E-value: 5.80e-04
                           10        20
                   ....*....|....*....|..
gi 939220313   425 RCPHCDRTFNPKAFDRHVEWCK 446
Cdd:pfam13913    4 PCPICGRTFNPDRLAKHEKICK 25
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1055-1167 1.04e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1055 NMSGMTDVSSQHEEKQSRQAEI-EKQTRLAEIEKQnrLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEK-QNRLAELet 1132
Cdd:COG4717    69 NLKELKELEEELKEAEEKEEEYaELQEELEELEEE--LEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAEL-- 144

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 939220313 1133 QSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREI 1167
Cdd:COG4717   145 PERLEELEERLEELRELEEELEELEAELAELQEEL 179
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1065-1153 1.06e-03

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: 43.57  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1065 QHEEKQSRQAEIEKQTR-LAEIEKQNRL---AEIEKQSR-LAEIEKQSRLAELEMQtrlaemEKQNRLAElETQSRLAEL 1139
Cdd:pfam17380  468 QEEERKRKKLELEKEKRdRKRAEEQRRKileKELEERKQaMIEEERKRKLLEKEME------ERQKAIYE-EERRREAEE 540

                           90
                   ....*....|....
gi 939220313  1140 EKRAAAEDQQKREI 1153
Cdd:pfam17380  541 ERRKQQEMEERRRI 554
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1065-1145 1.27e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEK-QTRLAEIEK--------------QNRLAEIEKQsrLAEIEKQ-----SRLAELEmqTRLAEMEKQ 1124
Cdd:COG4717   393 QAEEYQELKEELEElEEQLEELLGeleellealdeeelEEELEELEEE--LEELEEEleelrEELAELE--AELEQLEED 468

                          90       100
                  ....*....|....*....|....*.
gi 939220313 1125 NRLAELETQ-----SRLAELEKRAAA 1145
Cdd:COG4717   469 GELAELLQEleelkAELRELAEEWAA 494
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1067-1166 1.48e-03

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: 43.19  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1067 EEKQSRQAEIEKQTRLAEiEKQNRLAEIEKQSRLAEIEKqSRLAELEMQT-------RLAeMEKQNRLAELETQSRLAEL 1139
Cdd:pfam17380  286 ERQQQEKFEKMEQERLRQ-EKEEKAREVERRRKLEEAEK-ARQAEMDRQAaiyaeqeRMA-MERERELERIRQEERKREL 362

                           90       100       110
                   ....*....|....*....|....*....|.
gi 939220313  1140 EK----RAAAEDQQKREIfNRNSAEDQQKRE 1166
Cdd:pfam17380  363 ERirqeEIAMEISRMREL-ERLQMERQQKNE 392
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 1078-1160 1.51e-03

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 41.60  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1078 KQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLA---ELEMQTRLAEMEKQNRLAELETQSRLAELEkraaAEDQQKREIF 1154
Cdd:pfam01991    3 RQEAEEKAEEIRAKAEEEFAIEKAELVQEAEEKideIYEKKEKQAEMQKKIIISNAKNEARLKVLE----AREEILDEVF 78


                   ....*.
gi 939220313  1155 NRNSAE 1160
Cdd:pfam01991   79 NEAEKK 84
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1065-1152 1.76e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.63  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1065 QHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKqsrlAEIEKQsRLAELEMQ-----TRLAEMEKQNRLaELETQSRLAEL 1139
Cdd:pfam15709  415 QAAQERARQQQEEFRRKLQELQRKKQQEEAER----AEAEKQ-RQKELEMQlaeeqKRLMEMAEEERL-EYQRQKQEAEE 488

                           90
                   ....*....|...
gi 939220313  1140 EKRAAAEDQQKRE 1152
Cdd:pfam15709  489 KARLEAEERRQKE 501
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 1068-1167 2.23e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.90  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1068 EKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELE--TQSRLAEL-EKRAA 1144
Cdd:pfam12128  661 EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaLDAQLALLkAAIAA 740

                           90       100
                   ....*....|....*....|...
gi 939220313  1145 AEDQQKREIfnrNSAEDQQKREI 1167
Cdd:pfam12128  741 RRSGAKAEL---KALETWYKRDL 760
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1067-1153 2.43e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1067 EEKQSRQAEIEKQTRL-AEIEKQNRL-AEIEKQSRLAEIEKQSRLAE--LEMQTRLAEMEKQNRLAELETQSRLAELEKR 1142
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLrEEIDEFNEEqAEWKELEKEEEREEDERILEylKEKAEREEEREAEREEIEEEKEREIARLRAQ 192

                           90
                   ....*....|.
gi 939220313  1143 AAAEDQQKREI 1153
Cdd:pfam13868  193 QEKAQDEKAER 203
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1067-1177 2.47e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.45  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1067 EEKQSRQAEIEK-QTRLAEIEKQNRLAEIEKQSRLAEIEK-QSRLAEL----EMQTRLAEMEKQNRL------AELETQS 1134
Cdd:COG1579    38 DELAALEARLEAaKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVrnnkEYEALQKEIESLKRRisdledEILELME 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 939220313 1135 RLAELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANA 1177
Cdd:COG1579   118 RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1068-1177 2.54e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1068 EKQSRQAEIEKQTRLAEIEKQN-RLAEIE-----KQSRLAEIEKQSRLAE----------------LEMQTRLAEMEKQN 1125
Cdd:TIGR02169  895 EAQLRELERKIEELEAQIEKKRkRLSELKakleaLEEELSEIEDPKGEDEeipeeelsledvqaelQRVEEEIRALEPVN 974

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 939220313  1126 RLAELE---TQSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANA 1177
Cdd:TIGR02169  975 MLAIQEyeeVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINE 1029
zinc_ribbon_2 pfam13240
zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as ...
 1523-1543 2.58e-03

zinc-ribbon domain; This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR. pfam12773.


Pssm-ID: 433054 [Multi-domain]  Cd Length: 21  Bit Score: 36.71  E-value: 2.58e-03
                           10        20
                   ....*....|....*....|.
gi 939220313  1523 FCHECGAKfIVEQAKFCMECG 1543
Cdd:pfam13240    1 FCPNCGAE-NPDGAKFCPKCG 20
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1051-1177 2.62e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1051 RSDSNMSGMTDVSSQHEEKQSRQAEIEKqtrlaEIEKQNRLAEiEKQSRLAEIEkQSRLAELEMQTRLAEM--EKQNRLA 1128
Cdd:TIGR02169  703 RLDELSQELSDASRKIGEIEKEIEQLEQ-----EEEKLKERLE-ELEEDLSSLE-QEIENVKSELKELEARieELEEDLH 775

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 939220313  1129 ELETQsrLAELEKRAAAED-QQKREIFNRNSAEDQQKREIFISIETEANA 1177
Cdd:TIGR02169  776 KLEEA--LNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1059-1178 2.86e-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: 41.75  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1059 MTDVSSQHEEKQSRQAEIEKQTRlAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEK---QNRLAELETQSR 1135
Cdd:TIGR02794   42 LVDPGAVAQQANRIQQQKKPAAK-KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKqaeQAAKQAEEKQKQ 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 939220313  1136 LAELEKRAAAEDQQKREifnrNSAEDQQKREIFISIETEANAQ 1178
Cdd:TIGR02794  121 AEEAKAKQAAEAKAKAE----AEAERKAKEEAAKQAEEEAKAK 159
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1072-1167 3.99e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1072 RQAEIEKqtrlAEIEKQNRL--AEIEKQSRLAEIEKQSRLAELEMQTrlAEMEKQNRLAELETQSRLAELEKRAAAEDQQ 1149
Cdd:COG2268   199 RDARIAE----AEAERETEIaiAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEERREAETARAEAEAAYEIAE 272

                          90       100
                  ....*....|....*....|.
gi 939220313 1150 ---KREIfNRNSAEDQQKREI 1167
Cdd:COG2268   273 anaEREV-QRQLEIAEREREI 292
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1068-1166 4.21e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1068 EKQSRQAEIEKQTRLAEIEKQNRLAEI-EKQSRlaEIEKQSRLAELEMQTRLAEMEKQNRLAELEtqsrlaELEKRAaae 1146
Cdd:pfam13868  163 EKAEREEEREAEREEIEEEKEREIARLrAQQEK--AQDEKAERDELRAKLYQEEQERKERQKERE------EAEKKA--- 231

                           90       100
                   ....*....|....*....|
gi 939220313  1147 dQQKREIFNRNSAEDQQKRE 1166
Cdd:pfam13868  232 -RQRQELQQAREEQIELKER 250
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1057-1167 5.96e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1057 SGMTDVSSQHEEKQSRQAEIEKQTRLAEI-EKQNRLAEIEKQsrLAEIEKqsRLAELemQTRLAEMEKQNRLAEL----- 1130
Cdd:COG4717    62 QGRKPELNLKELKELEEELKEAEEKEEEYaELQEELEELEEE--LEELEA--ELEEL--REELEKLEKLLQLLPLyqele 135

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 939220313 1131 ETQSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREI 1167
Cdd:COG4717   136 ALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1083-1166 6.00e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1083 AEIEKQNRLAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELEtQSRLAELEKRAAAEDQQKREIFNRNSAEDQ 1162
Cdd:PRK09510   59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEA 137


                  ....
gi 939220313 1163 QKRE 1166
Cdd:PRK09510  138 AAKA 141
PTZ00121 PTZ00121
MAEBL; Provisional
 964-1174 6.32e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  964 VQHAHSNMPTFDDFDFEEFLSSFENENDDEQFPLFKDCREfllnRSTSRQRSFQKATSTPQPTATQQQHHHNNQSNNNHK 1043
Cdd:PTZ00121 1066 VGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKK----TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK 1141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1044 SKDVHAHRSDSNMSGMTDVSSQHEEKQSRQAE----IEKQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELEmQTRLA 1119
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAE-EARKA 1220

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 939220313 1120 EMEKQNRLAELETQSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETE 1174
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1059-1152 6.79e-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: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1059 MTDVSSQHEEKQSRQAEIEK---QTRLAEIEKQNR---LAEIEKQSRLAEIEKQSRLAELEMQTRLAEMEKQNRLAELET 1132
Cdd:pfam13868  186 IARLRAQQEKAQDEKAERDElraKLYQEEQERKERqkeREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFER 265

                           90       100
                   ....*....|....*....|.
gi 939220313  1133 QSR-LAELEKRAAAEDQQKRE 1152
Cdd:pfam13868  266 MLRkQAEDEEIEQEEAEKRRM 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1068-1165 6.94e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1068 EKQSRQAE--IEKQTRLAEIEK---------------QNRLAEIEKQSRLAEIEKQSRLAELEM-QTRLAEMEKQNRLAE 1129
Cdd:TIGR02168  206 ERQAEKAEryKELKAELRELELallvlrleelreeleELQEELKEAEEELEELTAELQELEEKLeELRLEVSELEEEIEE 285

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 939220313  1130 LetQSRLAELEKRAAAEDQQKREI-FNRNSAEDQQKR 1165
Cdd:TIGR02168  286 L--QKELYALANEISRLEQQKQILrERLANLERQLEE 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1061-1299 7.41e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1061 DVSSQHEEKQSRQAEI-EKQTRLAEIEKqnRLAEIEKqsrlaEIEKQSRLAELEMQTRLAEMEKQnrLAELETQSRLAEL 1139
Cdd:TIGR02169  245 QLASLEEELEKLTEEIsELEKRLEEIEQ--LLEELNK-----KIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1140 EKRAAAEDQQKreIFNRNSAEDQQKREIFISIETEAnaqgrspISPDSLRHMVGNSQTPIDVLHIENGNEPEHAR--FSK 1217
Cdd:TIGR02169  316 ELEDAEERLAK--LEAEIDKLLAEIEELEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAetRDE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1218 ISDTEDAGEEPGDRPSQLNSN------RLVQSSSSCALAPNvQLNNAKNLIQKMQSDFRQLGEEASASMRRTLIANSGRS 1291
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKREldrlqeELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465


                   ....*...
gi 939220313  1292 EEQQQMRD 1299
Cdd:TIGR02169  466 KYEQELYD 473
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1059-1186 8.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1059 MTDVSSQHEEKQSRQAEIEKQTRLAEIEKQNRLAEI--------EKQSRLAEIEKQSRLAELEMQT------RLAEMEKQ 1124
Cdd:COG4372   103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIaelqseiaEREEELKELEEQLESLQEELAAleqelqALSEAEAE 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939220313 1125 NRLAELETQSRLAELEKRAAAEDQQKREIFNRNSAEDQQKREIFISIETEANAQGRSPISPD 1186
Cdd:COG4372   183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1065-1177 8.87e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 8.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313  1065 QHEEKQSRQAEIE---KQTRLAEIEKQNRLAEIEKQSRLAEIEKQSRLAELemqtrlaemEKQNRLAELETQSRLAELEK 1141
Cdd:pfam02463  317 KESEKEKKKAEKElkkEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---------LEQLEEELLAKKKLESERLS 387

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 939220313  1142 RAAAEDQQKREIFNRNSAEDQQKREIFISIETEANA 1177
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1065-1159 9.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1065 QHEEKQSRQAEIEKQTRLAEIEKQNRLAEIEKQSRLAEIEK-QSRLAELE-----MQTRLAEMEkqNRLAELETQSRLAE 1138
Cdd:COG4717   396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEElEEELEELEeeleeLREELAELE--AELEQLEEDGELAE 473

                          90       100
                  ....*....|....*....|.
gi 939220313 1139 LEKRAAAEDQQKREIFNRNSA 1159
Cdd:COG4717   474 LLQELEELKAELRELAEEWAA 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1082-1167 1.00e-02

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.00e-02
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939220313 1082 LAEIEKQnrLAEIEKQSRLAE--IEKQSRLAELEMQTRLAEMEK-QNRLAELEtqsrlAELEKRAAAEDQQKREIFNRNS 1158
Cdd:COG1196   195 LGELERQ--LEPLERQAEKAEryRELKEELKELEAELLLLKLRElEAELEELE-----AELEELEAELEELEAELAELEA 267


                  ....*....
gi 939220313 1159 AEDQQKREI 1167
Cdd:COG1196   268 ELEELRLEL 276
 
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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