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Conserved domains on  [gi|157821009|ref|NP_001100241|]
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ankyrin repeat domain-containing protein 24 [Rattus norvegicus]

Protein Classification

ANKYR and Smc domain-containing protein( domain architecture ID 12790620)

ANKYR and Smc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-254 2.74e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  18 KSDQRLLQAVENNDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYG 97
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  98 HPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAA 177
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 178 ANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLLQESAQRPSPPNASLEDD 254
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
249-805 1.71e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 249 ASLEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLESERGNTSYEEEGEmpdfpgAEALlsknpspsgEE 328
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL------EEEL---------AE 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 329 IVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEEsqpevvpLVLYESLRAELQQLQRQHTEAMHMLQLQQGEPSG 408
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-------LLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 409 THGGEETAYQEIKDKGITIQNGLGVQDLNGTTYTEATANEMEPQAGGSKGVGNTEAGASEAALIEPEAVGSEAKGKDGVA 488
Cdd:COG1196  401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 489 AEAMDTSVTIAEALNVKSVGDNAEREPVTAEDTGGKENPGMKADGVDVLQAGLTGTVTRNMEATGVRdtgIQATGVEATA 568
Cdd:COG1196  481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA---LQNIVVEDDE 557
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 569 VKTTGVQATVAEVIGvkvtgvqttAAEAIGVNNTTAEATEAEATGAQANCSKATEADSTGAQDTAMEPTRAQATVLDTTE 648
Cdd:COG1196  558 VAAAAIEYLKAAKAG---------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 649 AETNGTEDHCAAILHPGAAAAALQAELESRIRALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEALREL 728
Cdd:COG1196  629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 729 LATATATGERARTEAAELRQQLAASEARVAELssaQDAAREELERMRGASVPADEhehALDALRDHVARLQAQLADL 805
Cdd:COG1196  709 LAEAEEERLEEELEEEALEEQLEAEREELLEE---LLEEEELLEEEALEELPEPP---DLEELERELERLEREIEAL 779
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-254 2.74e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  18 KSDQRLLQAVENNDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYG 97
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  98 HPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAA 177
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 178 ANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLLQESAQRPSPPNASLEDD 254
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 7.85e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   90 LHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSfkaHMKPRDR-SGATPLIIAAQMCHTDLC 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKdNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 157821009  169 RLLLQQGAAANDQD 182
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
50-209 2.53e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.68  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  50 DPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAG 129
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 130 GCLSCSKLLCSFKAHMKPrdRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGA 209
Cdd:PLN03192 602 KHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
249-805 1.71e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 249 ASLEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLESERGNTSYEEEGEmpdfpgAEALlsknpspsgEE 328
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL------EEEL---------AE 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 329 IVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEEsqpevvpLVLYESLRAELQQLQRQHTEAMHMLQLQQGEPSG 408
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-------LLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 409 THGGEETAYQEIKDKGITIQNGLGVQDLNGTTYTEATANEMEPQAGGSKGVGNTEAGASEAALIEPEAVGSEAKGKDGVA 488
Cdd:COG1196  401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 489 AEAMDTSVTIAEALNVKSVGDNAEREPVTAEDTGGKENPGMKADGVDVLQAGLTGTVTRNMEATGVRdtgIQATGVEATA 568
Cdd:COG1196  481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA---LQNIVVEDDE 557
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 569 VKTTGVQATVAEVIGvkvtgvqttAAEAIGVNNTTAEATEAEATGAQANCSKATEADSTGAQDTAMEPTRAQATVLDTTE 648
Cdd:COG1196  558 VAAAAIEYLKAAKAG---------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 649 AETNGTEDHCAAILHPGAAAAALQAELESRIRALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEALREL 728
Cdd:COG1196  629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 729 LATATATGERARTEAAELRQQLAASEARVAELssaQDAAREELERMRGASVPADEhehALDALRDHVARLQAQLADL 805
Cdd:COG1196  709 LAEAEEERLEEELEEEALEEQLEAEREELLEE---LLEEEELLEEEALEELPEPP---DLEELERELERLEREIEAL 779
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
59-189 3.31e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  59 LAAMRGSAGCLEVML-AQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEAS-CMVDVEDSS----GWTALHHAAAGGCL 132
Cdd:cd22192   23 LAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHIAVVNQNL 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821009 133 SCSKLLCSFKAHM-KPRDRS-------------GATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTAL 189
Cdd:cd22192  103 NLVRELIARGADVvSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
234-816 9.99e-06

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: 49.67  E-value: 9.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   234 LQLLQESAQRPSPPNASLEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLS-----LLESERGNTSYEEEgem 308
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeLEELESRLEELEEQ--- 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   309 pdfpgAEALLSKnpspsgeeiVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEESQPEVVPLVLYE------SLR 382
Cdd:TIGR02168  381 -----LETLRSK---------VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleELE 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   383 AELQQLQRQHTEAMHMLQLQQGEPSGTHGGEETAYQEIKDKGITIqNGLGVQDLNGTTYTEATANEMEPQAGGSKGVGnt 462
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGLSGILG-- 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   463 eagaSEAALIEPEAvgseakgKDGVAAEAmdtsvTIAEALN-VKSVGDNAERepvtaedtggkenpgmkaDGVDVLQAGL 541
Cdd:TIGR02168  524 ----VLSELISVDE-------GYEAAIEA-----ALGGRLQaVVVENLNAAK------------------KAIAFLKQNE 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   542 TGTVTRnMEATGVRDTGIQATGVEATAvKTTGVQATVAEVI---------------GVKVTGVQTTAAEAI-----GVNN 601
Cdd:TIGR02168  570 LGRVTF-LPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVkfdpklrkalsyllgGVLVVDDLDNALELAkklrpGYRI 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   602 TTAEATEAEATGAQANCSKATEAdSTGAQDTAMEPTRAQatvLDTTEAETNGTEDHCAAILHpgaaAAALQAELESRIRA 681
Cdd:TIGR02168  648 VTLDGDLVRPGGVITGGSAKTNS-SILERRREIEELEEK---IEELEEKIAELEKALAELRK----ELEELEEELEQLRK 719
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   682 LEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSR---ELEALRELLATATATGERARTEAAELRQQLAASEARVA 758
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821009   759 ELSSAQDAAREELERMRGAsvpADEHEHALDALRDHVARLQAQLADLARRHEKTSAEV 816
Cdd:TIGR02168  800 ALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
23-206 1.07e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   23 LLQAVENNDVARVASLIAHKGLVPTKLDP-------------EGKSAFHLAAMRGSAGCLEVMLAQGADV---------M 80
Cdd:TIGR00870  85 LLHAISLEYVDAVEAILLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVparacgdffV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   81 STDGAGY-----NALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAaggclscskllcsfkahMKPRDRSGATP 155
Cdd:TIGR00870 165 KSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------------MENEFKAEYEE 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009  156 LiiaAQMC------HTDLCRLLLQQGAAANdqdLQGRTALMLACEGGSPETVEVLLQ 206
Cdd:TIGR00870 228 L---SCQMynfalsLLDKLRDSKELEVILN---HQGLTPLKLAAKEGRIVLFRLKLA 278
PRK09039 PRK09039
peptidoglycan -binding protein;
259-394 7.63e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 259 SSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLESERG--NTSYEE-EGEMPDFPGAEALLS------KNPSPSGEEI 329
Cdd:PRK09039  59 NSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSrlQALLAElAGAGAAAEGRAGELAqeldseKQVSARALAQ 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821009 330 VASLQEQVAQLTRQNQELLEKVQILEefEKDEAQlveESQPEVVPLVLYESLRAELQQLQRQHTE 394
Cdd:PRK09039 139 VELLNQQIAALRRQLAALEAALDASE--KRDRES---QAKIADLGRRLNVALAQRVQELNRYRSE 198
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-114 8.80e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.80e-04
                           10        20
                   ....*....|....*....|....*....
gi 157821009    86 GYNALHLAAKYGHPECLKQLLEASCMVDV 114
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
720-846 1.33e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  720 RELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSA--QDAAREELERMRGASVPADEHEHALDALRDHVAR 797
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKgnEELAREALAEKKSLEKQAEALETQLAQQRSAVEQ 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157821009  798 LQAQLADLARRHEKTSAEvfqevftlKEALKVQQSTPASSKEQEEALRG 846
Cdd:pfam04012 116 LRKQLAALETKIQQLKAK--------KNLLKARLKAAKAQEAVQTSLGS 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-254 2.74e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  18 KSDQRLLQAVENNDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYG 97
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  98 HPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAA 177
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 178 ANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLLQESAQRPSPPNASLEDD 254
Cdd:COG0666  212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-258 1.88e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  23 LLQAVENNDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECL 102
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 103 KQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQD 182
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157821009 183 LQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLLQESAQRPSPPNASLEDDSGEA 258
Cdd:COG0666  184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-237 1.93e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 1.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  33 ARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMV 112
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 113 DVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLA 192
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157821009 193 CEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLL 237
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-189 1.85e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  23 LLQAVENNDVARVASLIAHkGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECL 102
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 103 KQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQD 182
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                 ....*..
gi 157821009 183 LQGRTAL 189
Cdd:COG0666  283 LDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-182 7.85e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   90 LHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSfkaHMKPRDR-SGATPLIIAAQMCHTDLC 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKdNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 157821009  169 RLLLQQGAAANDQD 182
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-149 9.89e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 9.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   57 FHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEaSCMVDVEDsSGWTALHHAAAGGCLSCSK 136
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 157821009  137 LLCSFKAHMKPRD 149
Cdd:pfam12796  79 LLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
50-209 2.53e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.68  E-value: 2.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  50 DPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAG 129
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 130 GCLSCSKLLCSFKAHMKPrdRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGA 209
Cdd:PLN03192 602 KHHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02875 PHA02875
ankyrin repeat protein; Provisional
26-213 2.93e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  26 AVENNDVARVASLIAHkGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGA---DVMSTDGAgyNALHLAAKYGHPECL 102
Cdd:PHA02875  42 AMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIM 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 103 KQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQD 182
Cdd:PHA02875 119 KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFG 198
                        170       180       190
                 ....*....|....*....|....*....|..
gi 157821009 183 LQGRTALM-LACEGGSPETVEVLLQGGAQLGI 213
Cdd:PHA02875 199 KNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
50-220 1.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  50 DPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAG 129
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 130 GCLSCSKLLCSFKAHMKPRDRSGATPLIIAaqMCHTDLCRLLLQQGAAANDQDLQGRTALMLACE-GGSPETVEVLLQGG 208
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHK 278
                        170
                 ....*....|..
gi 157821009 209 AQLGITDALGQD 220
Cdd:PHA02874 279 ADISIKDNKGEN 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-237 2.65e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  156 LIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDalGQDATHYGALTGDKLILQ 235
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                  ..
gi 157821009  236 LL 237
Cdd:pfam12796  79 LL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
62-224 5.55e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  62 MRGSAGCLEVM---LAQGADVMSTDGAGYNALHLAAKYGHPECLK---QLLEASCMVDVEDSSGWTALHhaaaggCLSCS 135
Cdd:PHA03095  20 LNASNVTVEEVrrlLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLH------LYLYN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 136 -------KLLCSFKAHMKPRDRSGATPL-IIAAQMC-HTDLCRLLLQQGAAANDQDLQGRTAL--MLACEGGSPETVEVL 204
Cdd:PHA03095  94 attldviKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLL 173
                        170       180
                 ....*....|....*....|
gi 157821009 205 LQGGAQLGITDALGQDATHY 224
Cdd:PHA03095 174 IDAGADVYAVDDRFRSLLHH 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
35-192 7.72e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  35 VASLIAhKGLVPTKLDPEGKSAfhLAAMRGSAGC----LEVMLAQGADVMSTDGAGYNALHLAAKYGHP--ECLKQLLEA 108
Cdd:PHA03095 135 IRLLLR-KGADVNALDLYGMTP--LAVLLKSRNAnvelLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRA 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 109 SCMVDVEDSSGWTALHHAAAGGclSCSKLLCSF----KAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQ 184
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                 ....*...
gi 157821009 185 GRTALMLA 192
Cdd:PHA03095 290 GNTPLSLM 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-126 1.54e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157821009   77 ADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHA 126
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
31-233 3.25e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  31 DVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGS-AGCLEVMLAQGADVMSTDGAGYNALH--LAAKYGHPECLKQLLE 107
Cdd:PHA03095  61 KVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 108 ASCMVDVEDSSGWTALH-----HAAaggCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLC--RLLLQQGAAAND 180
Cdd:PHA03095 141 KGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAA 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 181 QDLQGRTALMLACEGGSPETVEV--LLQGGAQLGITDALGQDATHYGALTG-----DKLI 233
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNnpracRRLI 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
154-205 4.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 4.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157821009  154 TPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLL 205
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 7.57e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 7.57e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157821009   86 GYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
30-180 1.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  30 NDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMR--GSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPEC------ 101
Cdd:PHA03100  83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkll 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 102 ------------LKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCR 169
Cdd:PHA03100 163 idkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242
                        170
                 ....*....|.
gi 157821009 170 LLLQQGAAAND 180
Cdd:PHA03100 243 LLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
69-237 9.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 9.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  69 LEVMLAQGADVMSTDGAGYNALHLAA--KYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGGC--LSCSKLLCSFKAH 144
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVD 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 145 MKPRDRsgatpliiaaqmchtdlCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHY 224
Cdd:PHA03100 169 INAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
                        170
                 ....*....|...
gi 157821009 225 GALTGDKLILQLL 237
Cdd:PHA03100 232 AILNNNKEIFKLL 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
100-211 1.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 100 ECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAAN 179
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                         90       100       110
                 ....*....|....*....|....*....|..
gi 157821009 180 DQDLQGRTALMLACEGGSPETVEVLLQGGAQL 211
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
44-206 2.10e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  44 LVPTKLDPE-----GKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEdsS 118
Cdd:PLN03192 544 LLKAKLDPDigdskGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--A 621
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 119 GWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQgrtalmlacEGGSP 198
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD---------DDFSP 692

                 ....*...
gi 157821009 199 ETVEVLLQ 206
Cdd:PLN03192 693 TELRELLQ 700
PHA02876 PHA02876
ankyrin repeat protein; Provisional
31-223 4.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  31 DVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASC 110
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 111 MVDVEDSSgwtaLHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMchTDLCRL---LLQQGAAANDQDLQGRT 187
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA--PSLSRLvpkLLERGADVNAKNIKGET 309
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 157821009 188 ALMLACEGG-SPETVEVLLQGGAQLGITDALGQDATH 223
Cdd:PHA02876 310 PLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLH 346
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-106 7.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 7.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157821009   55 SAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLL 106
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
119-172 1.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157821009  119 GWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLL 172
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
249-805 1.71e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 249 ASLEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLESERGNTSYEEEGEmpdfpgAEALlsknpspsgEE 328
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL------EEEL---------AE 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 329 IVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEEsqpevvpLVLYESLRAELQQLQRQHTEAMHMLQLQQGEPSG 408
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-------LLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 409 THGGEETAYQEIKDKGITIQNGLGVQDLNGTTYTEATANEMEPQAGGSKGVGNTEAGASEAALIEPEAVGSEAKGKDGVA 488
Cdd:COG1196  401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 489 AEAMDTSVTIAEALNVKSVGDNAEREPVTAEDTGGKENPGMKADGVDVLQAGLTGTVTRNMEATGVRdtgIQATGVEATA 568
Cdd:COG1196  481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA---LQNIVVEDDE 557
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 569 VKTTGVQATVAEVIGvkvtgvqttAAEAIGVNNTTAEATEAEATGAQANCSKATEADSTGAQDTAMEPTRAQATVLDTTE 648
Cdd:COG1196  558 VAAAAIEYLKAAKAG---------RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 649 AETNGTEDHCAAILHPGAAAAALQAELESRIRALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEALREL 728
Cdd:COG1196  629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009 729 LATATATGERARTEAAELRQQLAASEARVAELssaQDAAREELERMRGASVPADEhehALDALRDHVARLQAQLADL 805
Cdd:COG1196  709 LAEAEEERLEEELEEEALEEQLEAEREELLEE---LLEEEELLEEEALEELPEPP---DLEELERELERLEREIEAL 779
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
59-189 3.31e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  59 LAAMRGSAGCLEVML-AQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEAS-CMVDVEDSS----GWTALHHAAAGGCL 132
Cdd:cd22192   23 LAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHIAVVNQNL 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821009 133 SCSKLLCSFKAHM-KPRDRS-------------GATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTAL 189
Cdd:cd22192  103 NLVRELIARGADVvSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
251-828 5.42e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 5.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 251 LEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLE---SERGNTSYEEEGEMPDFPGAEALLsknpspsgE 327
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElelEEAQAEEYELLAELARLEQDIARL--------E 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 328 EIVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEESQPEVvplvlyESLRAELQQLQRQHTEAMHMLQLQQGEps 407
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL------EEAEAELAEAEEALLEAEAELAEAEEE-- 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 408 gthggEETAYQEIkdkgitiqnglgvqdlngttytEATANEMEPQAGGSKGVGNTEAGASEAALIEPEAVGSEAKGKDGV 487
Cdd:COG1196  381 -----LEELAEEL----------------------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 488 AAEAMDTSVTIAEALNVKSVGDNAEREPVTAEDTGGKENPGMKADGVDVLQAGLTGTVTRNMEATGVRDTGIQATGVEAT 567
Cdd:COG1196  434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 568 AVKT--TGVQATVAEVIGVKVTGVQTTAAEAIGVNNTTAEATEAEATGAQANCSKATEADSTGAQDTAMEPTRAQAtvld 645
Cdd:COG1196  514 LLLAglRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA---- 589
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 646 ttEAETNGTEDHCAAILHPGAAAAALQAELESRIRALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEAL 725
Cdd:COG1196  590 --AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 726 RELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGASVPADEHEHALDALRDHVARLQAQLADL 805
Cdd:COG1196  668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
                        570       580
                 ....*....|....*....|...
gi 157821009 806 ARRHEKTSAEVFQEVFTLKEALK 828
Cdd:COG1196  748 LEEEALEELPEPPDLEELERELE 770
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
234-816 9.99e-06

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: 49.67  E-value: 9.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   234 LQLLQESAQRPSPPNASLEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQSRLS-----LLESERGNTSYEEEgem 308
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaeLEELESRLEELEEQ--- 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   309 pdfpgAEALLSKnpspsgeeiVASLQEQVAQLTRQNQELLEKVQILEEFEKDEAQLVEESQPEVVPLVLYE------SLR 382
Cdd:TIGR02168  381 -----LETLRSK---------VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleELE 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   383 AELQQLQRQHTEAMHMLQLQQGEPSGTHGGEETAYQEIKDKGITIqNGLGVQDLNGTTYTEATANEMEPQAGGSKGVGnt 462
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGLSGILG-- 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   463 eagaSEAALIEPEAvgseakgKDGVAAEAmdtsvTIAEALN-VKSVGDNAERepvtaedtggkenpgmkaDGVDVLQAGL 541
Cdd:TIGR02168  524 ----VLSELISVDE-------GYEAAIEA-----ALGGRLQaVVVENLNAAK------------------KAIAFLKQNE 569
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   542 TGTVTRnMEATGVRDTGIQATGVEATAvKTTGVQATVAEVI---------------GVKVTGVQTTAAEAI-----GVNN 601
Cdd:TIGR02168  570 LGRVTF-LPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVkfdpklrkalsyllgGVLVVDDLDNALELAkklrpGYRI 647
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   602 TTAEATEAEATGAQANCSKATEAdSTGAQDTAMEPTRAQatvLDTTEAETNGTEDHCAAILHpgaaAAALQAELESRIRA 681
Cdd:TIGR02168  648 VTLDGDLVRPGGVITGGSAKTNS-SILERRREIEELEEK---IEELEEKIAELEKALAELRK----ELEELEEELEQLRK 719
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   682 LEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSR---ELEALRELLATATATGERARTEAAELRQQLAASEARVA 758
Cdd:TIGR02168  720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821009   759 ELSSAQDAAREELERMRGAsvpADEHEHALDALRDHVARLQAQLADLARRHEKTSAEV 816
Cdd:TIGR02168  800 ALREALDELRAELTLLNEE---AANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
PHA02878 PHA02878
ankyrin repeat protein; Provisional
38-215 1.45e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  38 LIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDS 117
Cdd:PHA02878 153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 118 SGWTALHHaAAGGCLScskllcsfkahmkprdrsgatpliiaaqmchTDLCRLLLQQGAAANDQD-LQGRTALMLACEgg 196
Cdd:PHA02878 233 CGNTPLHI-SVGYCKD-------------------------------YDILKLLLEHGVDVNAKSyILGLTALHSSIK-- 278
                        170
                 ....*....|....*....
gi 157821009 197 SPETVEVLLQGGAQLGITD 215
Cdd:PHA02878 279 SERKLKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
33-126 1.61e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  33 ARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEV--MLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASC 110
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
                         90
                 ....*....|....*.
gi 157821009 111 MVDVEDSSGWTALHHA 126
Cdd:PHA03095 282 DINAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-244 2.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  60 AAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAA-GGCLSCSKLL 138
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEeGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 139 CSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALG 218
Cdd:PHA02875  89 DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                        170       180
                 ....*....|....*....|....*.
gi 157821009 219 QDATHYGALTGDKLILQLLQESAQRP 244
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANI 194
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
716-851 2.33e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  716 RGRSRELEALRELLA--TATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGA--SVPADEhehaLDAL 791
Cdd:COG4913   268 RERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDR----LEQL 343
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  792 RDHVARLQAQLADLARRHEKtsaevfqevftLKEALKVQQSTPASSKEQEEALRGQVTAL 851
Cdd:COG4913   344 EREIERLERELEERERRRAR-----------LEALLAALGLPLPASAEEFAALRAEAAAL 392
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
123-205 2.80e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 123 LHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVE 202
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ...
gi 157821009 203 VLL 205
Cdd:PTZ00322 166 LLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
38-93 4.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157821009   38 LIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLA 93
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
677-851 4.74e-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: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 677 SRIRALEEALRRREQEaAAELEAARGRFAQAEAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQQLAASEAR 756
Cdd:COG1196  295 AELARLEQDIARLEER-RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 757 VAELSSAQDAAREELERMRGASVPADEHEHALDALRDHVARLQAQLADLARRHEKTSAEVFQEVFTLKEALKVQQSTPAS 836
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        170
                 ....*....|....*
gi 157821009 837 SKEQEEALRGQVTAL 851
Cdd:COG1196  454 LEEEEEALLELLAEL 468
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
23-206 1.07e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   23 LLQAVENNDVARVASLIAHKGLVPTKLDP-------------EGKSAFHLAAMRGSAGCLEVMLAQGADV---------M 80
Cdd:TIGR00870  85 LLHAISLEYVDAVEAILLHLLAAFRKSGPlelandqytseftPGITALHLAAHRQNYEIVKLLLERGASVparacgdffV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   81 STDGAGY-----NALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAaggclscskllcsfkahMKPRDRSGATP 155
Cdd:TIGR00870 165 KSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------------MENEFKAEYEE 227
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157821009  156 LiiaAQMC------HTDLCRLLLQQGAAANdqdLQGRTALMLACEGGSPETVEVLLQ 206
Cdd:TIGR00870 228 L---SCQMynfalsLLDKLRDSKELEVILN---HQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
160-265 1.47e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 160 AQMCHTDLC-----------RLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALT 228
Cdd:PTZ00322  79 AHMLTVELCqlaasgdavgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157821009 229 GDKLILQLLQESAQRPSPPNASLEDDSGEASSQVQEL 265
Cdd:PTZ00322 159 GFREVVQLLSRHSQCHFELGANAKPDSFTGKPPSLED 195
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
719-816 2.08e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  719 SRELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGASVPADE-------HEHALDAL 791
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleerfAAALGDAV 763
                          90       100
                  ....*....|....*....|....*.
gi 157821009  792 RDHVAR-LQAQLADLARRHEKTSAEV 816
Cdd:COG4913   764 ERELREnLEERIDALRARLNRAEEEL 789
PHA02878 PHA02878
ankyrin repeat protein; Provisional
136-224 2.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 136 KLLCSFKAHMKPRDR-SGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGIT 214
Cdd:PHA02878 151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230
                         90
                 ....*....|
gi 157821009 215 DALGQDATHY 224
Cdd:PHA02878 231 DKCGNTPLHI 240
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
52-183 2.72e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  52 EGKSAFHLAAMRGSAGCLEVMLAQGADV-MSTDGA------------GYNALHLAAKYGHPECLKQLLEASCM---VDVE 115
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVsARATGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 116 DSSGWTALH-------HAAAGGCLSCS--KLLCSFKAHMKP-------RDRSGATPLIIAAQMCHTDLCRLLLQQGAAAN 179
Cdd:cd21882  152 DSLGNTVLHalvlqadNTPENSAFVCQmyNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHILQREFSGP 231

                 ....
gi 157821009 180 DQDL 183
Cdd:cd21882  232 YQPL 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
717-851 2.98e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   717 GRSRELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRG----ASVPADEHEHALDALR 792
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821009   793 DHVARLQAQLADLARRHEKTS---AEVFQEVFTLKEALKVQQSTPASSKEQEEALRGQVTAL 851
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEeelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
Ank_4 pfam13637
Ankyrin repeats (many copies);
185-237 3.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157821009  185 GRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALTGDKLILQLL 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
720-886 3.41e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  720 RELEALRELLATATATGERARTEAAELRQQLAA---------SEARVAELSSAQDAAREELERMRGASVpadehehALDA 790
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASSD-------DLAA 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  791 LRDHVARLQAQLADLARRHEKTSaevfQEVFTLKEALkvqqstpASSKEQEEALRGQVTALQQQIQEEAQEHCTvvALYR 870
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELK----GEIGRLEKEL-------EQAEEELDELQDRLEAAEDLARLELRALLE--ERFA 756
                         170
                  ....*....|....*.
gi 157821009  871 THLLYAIQGQMDEDVQ 886
Cdd:COG4913   757 AALGDAVERELRENLE 772
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-83 3.67e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157821009   12 EGQDWGKSDQR----LLQAVENNDVARVASLIAHkglVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTD 83
Cdd:pfam12796  19 NGADANLQDKNgrtaLHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
35-159 4.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  35 VASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGYNALHLAAKYGhpECLKQLLEASCMVDV 114
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASIND 249
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157821009 115 EDSSGWTALHHAAAGGC-LSCSKLLCSFKAHMKPRDRSGATPLIIA 159
Cdd:PHA02874 250 QDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_5 pfam13857
Ankyrin repeats (many copies);
171-219 5.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 157821009  171 LLQQG-AAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQ 219
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL 50
PHA02876 PHA02876
ankyrin repeat protein; Provisional
72-211 6.46e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  72 MLAQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGGCLSCS-KLLCSFKAHMKPRDR 150
Cdd:PHA02876 361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNK 440
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821009 151 SGATPLIIAAQM-CHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSpeTVEVLLQGGAQL 211
Cdd:PHA02876 441 DLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
PRK09039 PRK09039
peptidoglycan -binding protein;
259-394 7.63e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 259 SSQVQELQQMLAEKQEEKESLGREVESLQSRLSLLESERG--NTSYEE-EGEMPDFPGAEALLS------KNPSPSGEEI 329
Cdd:PRK09039  59 NSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSrlQALLAElAGAGAAAEGRAGELAqeldseKQVSARALAQ 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821009 330 VASLQEQVAQLTRQNQELLEKVQILEefEKDEAQlveESQPEVVPLVLYESLRAELQQLQRQHTE 394
Cdd:PRK09039 139 VELLNQQIAALRRQLAALEAALDASE--KRDRES---QAKIADLGRRLNVALAQRVQELNRYRSE 198
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-114 8.80e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.80e-04
                           10        20
                   ....*....|....*....|....*....
gi 157821009    86 GYNALHLAAKYGHPECLKQLLEASCMVDV 114
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PRK09039 PRK09039
peptidoglycan -binding protein;
721-806 9.58e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 721 ELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGasvpadehehALDALRDHVARLQA 800
Cdd:PRK09039  82 SVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALA----------QVELLNQQIAALRR 151

                 ....*.
gi 157821009 801 QLADLA 806
Cdd:PRK09039 152 QLAALE 157
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
720-846 1.33e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  720 RELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSA--QDAAREELERMRGASVPADEHEHALDALRDHVAR 797
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKgnEELAREALAEKKSLEKQAEALETQLAQQRSAVEQ 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 157821009  798 LQAQLADLARRHEKTSAEvfqevftlKEALKVQQSTPASSKEQEEALRG 846
Cdd:pfam04012 116 LRKQLAALETKIQQLKAK--------KNLLKARLKAAKAQEAVQTSLGS 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
719-851 1.35e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   719 SRELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGASVPA----------------- 781
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrleeleeqletlrsk 387
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821009   782 -DEHEHALDALRDHVARLQAQLADLARRHEKTSAEVFQEVFTLKEA-LKVQQSTPASSKEQEEALRGQVTAL 851
Cdd:TIGR02168  388 vAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERL 459
PHA02874 PHA02874
ankyrin repeat protein; Provisional
148-237 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 148 RDRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGAL 227
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                         90
                 ....*....|
gi 157821009 228 TGDKLILQLL 237
Cdd:PHA02874 200 YGDYACIKLL 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
679-856 2.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 679 IRALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEALRELLATAtatgERARTEAAELRQQLAASEARVA 758
Cdd:COG1196  265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 759 ELSSAQDAAREELErmrgasvpadeheHALDALRDHVARLQAQLADLARRHEKTSAEVfQEVFTLKEALKVQQSTPASSK 838
Cdd:COG1196  341 ELEEELEEAEEELE-------------EAEAELAEAEEALLEAEAELAEAEEELEELA-EELLEALRAAAELAAQLEELE 406
                        170
                 ....*....|....*...
gi 157821009 839 EQEEALRGQVTALQQQIQ 856
Cdd:COG1196  407 EAEEALLERLERLEEELE 424
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
736-851 2.44e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  736 GERARTEAAELRQQLAASEARVAELSSAQDAAREELERMR------GASVPADEHEHALDALRDHVARLQAQLADLarrh 809
Cdd:COG4913   605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQerrealQRLAEYSWDEIDVASAEREIAELEAELERL---- 680
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 157821009  810 EKTSAEVFQevftLKEALKVQQSTPASSKEQEEALRGQVTAL 851
Cdd:COG4913   681 DASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRL 718
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
721-794 2.70e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821009  721 ELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGASVPADEHEHAL-DALRDH 794
Cdd:COG4913   378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrDALAEA 452
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
149-250 3.20e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 149 DRSGATPLIIAAQMCHTDLCRLLLQQGAAANDQDLQGRTALMLACEGGSPETVEVLLQGGAQLGITDALGQDATHYGALT 228
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISA 601
                         90       100
                 ....*....|....*....|..
gi 157821009 229 GDKLILQLLQESAqRPSPPNAS 250
Cdd:PLN03192 602 KHHKIFRILYHFA-SISDPHAA 622
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
721-828 3.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 721 ELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMR----GASVPADEHEHALDALRDHVA 796
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgDAPVDLGNAEDFLEELREERD 422
                         90       100       110
                 ....*....|....*....|....*....|..
gi 157821009 797 RLQAQLADLaRRHEKTSAEVFQEVFTLKEALK 828
Cdd:PRK02224 423 ELREREAEL-EATLRTARERVEEAEALLEAGK 453
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
52-161 3.57e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  52 EGKSAFHLAAMRGSAGCLEVMLAQGADVMSTDGAGY--------------NALHLAAKYGHPECLKQLLEASCMVDVEDS 117
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157821009 118 SGWTALHHAA--AGGCLSCS--KLLCSFKAHMKP------RDRSGATPLIIAAQ 161
Cdd:cd22192  168 LGNTVLHILVlqPNKTFACQmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAK 221
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
47-218 4.31e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009   47 TKLDPEGKsAFHLAAMRGSAGCLEVML--AQGADVMSTDGAGYNALHLAAKYGHPECLKQLLEA-SCMVDVEDssgwTAL 123
Cdd:TIGR00870  12 SPLSDEEK-AFLPAAERGDLASVYRDLeePKKLNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGD----TLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  124 HHAAAGGCLSCSKLLcsfkAHMKPRDRS-----------------GATPLIIAAQMCHTDLCRLLLQQGAAAN------- 179
Cdd:TIGR00870  87 HAISLEYVDAVEAIL----LHLLAAFRKsgplelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVParacgdf 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157821009  180 -----DQDL--QGRTALMLACEGGSPETVEVLLQGGAQLGITDALG 218
Cdd:TIGR00870 163 fvksqGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLG 208
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
184-215 4.44e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.44e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 157821009  184 QGRTALMLAC-EGGSPETVEVLLQGGAQLGITD 215
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
86-116 4.66e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 4.66e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157821009   86 GYNALHLAA-KYGHPECLKQLLEASCMVDVED 116
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
18-170 5.20e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  18 KSDQRL--LQAVENNDVARVASLIAHKGLVPTKLDPEGKSAFHLAAMRGSAGcLEVMLAQGADVMSTDGAGYNALHLAAK 95
Cdd:PTZ00322  46 RIDTHLeaLEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  96 YGHPECLKQLLEASCMVDVEDSSGWTALHHAAAGG-------CLSCSKLLCSFKAHMKPRDRSGATPLIIA--AQMCHTD 166
Cdd:PTZ00322 125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrevvqlLSRHSQCHFELGANAKPDSFTGKPPSLEDspISSHHPD 204

                 ....
gi 157821009 167 LCRL 170
Cdd:PTZ00322 205 FSAV 208
Ank_5 pfam13857
Ankyrin repeats (many copies);
105-159 5.55e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157821009  105 LLEA-SCMVDVEDSSGWTALHHAAAGGCLSCSKLLCSFKAHMKPRDRSGATPLIIA 159
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
152-182 6.02e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.02e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157821009  152 GATPLIIAAQMC-HTDLCRLLLQQGAAANDQD 182
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
251-287 6.14e-03

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 37.17  E-value: 6.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 157821009  251 LEDDSGEASSQVQELQQMLAEKQEEKESLGREVESLQ 287
Cdd:pfam14931  69 LKSEAKQREAEQQQLQALILEKKVELERLRVEYQSLQ 105
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
184-209 6.35e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 6.35e-03
                           10        20
                   ....*....|....*....|....*.
gi 157821009   184 QGRTALMLACEGGSPETVEVLLQGGA 209
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-392 6.87e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  209 AQLGITDALGQDATHYGAltgdKLILQLLQESAQRpsppnasLEDDSGEASSQVQELQQMLAEKQEEKESL--------G 280
Cdd:COG4913   269 ERLAELEYLRAALRLWFA----QRRLELLEAELEE-------LRAELARLEAELERLEARLDALREELDELeaqirgngG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  281 REVESLQSRLSLLESERGNTSYEEEgempdfpGAEALLS--KNPSPSGEEIVASLQEQVAQLTRQNQELLEKVQ-ILEEF 357
Cdd:COG4913   338 DRLEQLEREIERLERELEERERRRA-------RLEALLAalGLPLPASAEEFAALRAEAAALLEALEEELEALEeALAEA 410
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 157821009  358 EKDEAQLVEEsqpevvplvlYESLRAELQQLQRQH 392
Cdd:COG4913   411 EAALRDLRRE----------LRELEAEIASLERRK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
716-821 7.36e-03

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: 39.75  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 716 RGRSRELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGAsvpADEHEHALDALRDHV 795
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE---LAELAAELAELQQEA 222
                         90       100
                 ....*....|....*....|....*.
gi 157821009 796 ARLQAQLADLARRHEKTSAEVFQEVF 821
Cdd:COG4942  223 EELEALIARLEAEAAAAAERTPAAGF 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
185-213 7.37e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.37e-03
                          10        20
                  ....*....|....*....|....*....
gi 157821009  185 GRTALMLACEGGSPETVEVLLQGGAQLGI 213
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
680-846 7.68e-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: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 680 RALEEALRRREQEAAAELEAARGRFAQAEAEAEEAARGRSRELEALRELLATATATGERARTEAAELRQQLAASEARVAE 759
Cdd:COG1196  339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 760 LSSAQDAAREELERMRGASVPADEHEHALDALRDHVARLQAQLADLARRHEKTSAEVFQEVFTLKEALKVQQSTPASSKE 839
Cdd:COG1196  419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                 ....*..
gi 157821009 840 QEEALRG 846
Cdd:COG1196  499 AEADYEG 505
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
720-813 8.17e-03

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: 39.36  E-value: 8.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009 720 RELEALRELLATATATGERARTEAAELRQQLAASEARVAELSSAQDAAREELERMRGAsvpADEHEHALDALRDHVARLQ 799
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE---LAELEKEIAELRAELEAQK 103
                         90
                 ....*....|....
gi 157821009 800 AQLADLARRHEKTS 813
Cdd:COG4942  104 EELAELLRALYRLG 117
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
259-391 8.51e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 39.17  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821009  259 SSQVQELQQMLAEKQEEKESLGrevESLQSRLSLLESERGNTSyeeegempdfpgaEALLSKnpspSGEEIVASLQEQVA 338
Cdd:pfam15397 123 ANLVRQLQQLKDSQQDELDELE---EMRRMVLESLSRKIQKKK-------------EKILSS----LAEKTLSPYQESLL 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157821009  339 QLTRQNQELLEKvqiLEEFEKDEAQLVEEsqpevVPLvlyesLRAELQQLQRQ 391
Cdd:pfam15397 183 QKTRDNQVMLKE---IEQFREFIDELEEE-----IPK-----LKAEVQQLQAQ 222
 
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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