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Conserved domains on  [gi|2462564264|ref|XP_054176431|]
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KN motif and ankyrin repeat domain-containing protein 3 isoform X2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13778391)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions; similar to Homo sapiens ankyrin repeat and SOCS box protein 7 isoform 1; ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  15152081|17176038

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-786 1.10e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462564264 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
33-74 1.05e-16

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


:

Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.31  E-value: 1.05e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462564264  33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
58-586 5.26e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 50.26  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLYGEVGSLD 295
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDTSDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462564264  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-786 1.10e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462564264 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
33-74 1.05e-16

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.31  E-value: 1.05e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462564264  33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
627-726 1.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 627 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 706
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71
                          90       100
                  ....*....|....*....|
gi 2462564264 707 GRQDMVATLLACGADVNAQD 726
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
616-772 4.97e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 691
Cdd:PHA03095   40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 692 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 767
Cdd:PHA03095  114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191

                  ....*
gi 2462564264 768 AIALE 772
Cdd:PHA03095  192 HHHLQ 196
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
58-586 5.26e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 50.26  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLYGEVGSLD 295
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDTSDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462564264  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
622-647 2.25e-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: 39.11  E-value: 2.25e-04
                           10        20
                   ....*....|....*....|....*.
gi 2462564264  622 NGNTALHYSVSHGNLAIASLLLDTGA 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
623-778 4.79e-04

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: 43.85  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 623 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 695
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 696 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 762
Cdd:cd22192   125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190
                         170
                  ....*....|....*.
gi 2462564264 763 gtsaLAIALEAEQDEV 778
Cdd:cd22192   191 ----LILSYDKEDDLQ 202
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
188-287 2.97e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 41.14  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 188 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 263
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584
                          90       100
                  ....*....|....*....|....
gi 2462564264 264 RASPRADSPDGLAAGRSEGALQVL 287
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
PHA03247 PHA03247
large tegument protein UL36; Provisional
59-181 9.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264   59 PAARRAPGPPTSRRPRAPRPGlagarSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLRETS 138
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPD-----PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG 2693
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462564264  139 RRLELAQTHERAPSP---------GRGVPRSPRGSGRSSPAPNLAPASPGPA 181
Cdd:PHA03247  2694 SLTSLADPPPPPPTPepaphalvsATPLPPGPAAARQASPALPAAPAPPAVP 2745
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-786 1.10e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 1.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAA------YNGNL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666   134 EIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GAD 211
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462564264 756 PAILDNEGTSALAIALEAEQDEVAALLHAHL 786
Cdd:COG0666   212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
610-782 8.33e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 8.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 610 ELLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG- 686
Cdd:COG0666   105 LLLEAgaDVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGa 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 687 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSA 766
Cdd:COG0666   178 DVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTA 255
                         170
                  ....*....|....*.
gi 2462564264 767 LAIALEAEQDEVAALL 782
Cdd:COG0666   256 LLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
597-785 6.60e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 6.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 597 VARMLEGVRRLGPELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDM 676
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAA------RNGDL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 677 AVVQRLFCMG-DVNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCD 755
Cdd:COG0666   101 EIVKLLLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GAD 178
                         170       180       190
                  ....*....|....*....|....*....|
gi 2462564264 756 PAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-764 1.09e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 611 LLAH--VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 687
Cdd:COG0666   139 LLEAgaDVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaD 211
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462564264 688 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDPAILDNEGT 764
Cdd:COG0666   212 VNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
610-782 3.46e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 3.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 610 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGACEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVN 689
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAA------LAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 690 AKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAI 769
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159
                         170
                  ....*....|...
gi 2462564264 770 ALEAEQDEVAALL 782
Cdd:COG0666   160 AAANGNLEIVKLL 172
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
33-74 1.05e-16

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 74.31  E-value: 1.05e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462564264  33 PYSVETPYGFHLDLDFLKYIEELERGPAARRAPGPptsRRPR 74
Cdd:pfam12075   1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQ---RRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
627-726 1.10e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 627 LHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLAALTSVRQeeedmaVVQRLFCMGDVNAKASqtGQTALMLAISH 706
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLE------IVKLLLEHADVNLKDN--GRTALHYAARS 71
                          90       100
                  ....*....|....*....|
gi 2462564264 707 GRQDMVATLLACGADVNAQD 726
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
700-782 1.41e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 700 LMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCDpaiLDNEGTSALAIALEAEQDEVA 779
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                  ...
gi 2462564264 780 ALL 782
Cdd:pfam12796  78 KLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
661-760 3.55e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 661 LMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACgADVNAQDaDGATALMCASEY 739
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGaDANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARS 71
                          90       100
                  ....*....|....*....|.
gi 2462564264 740 GRLDTVRLLLtQPGCDPAILD 760
Cdd:pfam12796  72 GHLEIVKLLL-EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
660-785 1.75e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.83  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 660 ALMLAALTSVRQEEEDMAVVQRLFCMGDVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEY 739
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462564264 740 GRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:COG0666    98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
616-772 4.97e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSHGN---LAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVRQEeedmaVVQRLFCMG-DVNAK 691
Cdd:PHA03095   40 VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNATTLD-----VIKLLIKAGaDVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 692 aSQTGQTAL--MLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGR--LDTVRLLLTQpGCDPAILDNEGTSAL 767
Cdd:PHA03095  114 -DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLL 191

                  ....*
gi 2462564264 768 AIALE 772
Cdd:PHA03095  192 HHHLQ 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
698-749 1.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462564264 698 TALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 749
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
715-810 1.88e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 715 LLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAHlSSGQPDTQ 794
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH-SQCHFELG 178
                          90
                  ....*....|....*.
gi 2462564264 795 SESPPGSQTATPGEGE 810
Cdd:PTZ00322  179 ANAKPDSFTGKPPSLE 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
616-772 2.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMGDVNAKASQT 695
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YANVKDNNGESPLHNAA------EYGDYACIKLLIDHGNHIMNKCKN 222
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462564264 696 GQTALMLAISHGRQdmVATLLACGADVNAQDADGATALMCASEYG-RLDTVRLLLTQPGcDPAILDNEGTSALAIALE 772
Cdd:PHA02874  223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
617-811 4.12e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 617 NLADGNGNTALHYSVSHGNLAIASLLLDTgACEVNRQNRAGYSALMLAAltsvrqeeedMAVVQRLFCMGDVNAKAS--Q 694
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpH 620
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 695 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQ-PGCDPAILDNEGTSA-LAIALE 772
Cdd:PLN03192  621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNgADVDKANTDDDFSPTeLRELLQ 700
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462564264 773 AEQDEVAALLHAHLSSGQPDTQSE--SPPGSQTATPGEGEC 811
Cdd:PLN03192  701 KRELGHSITIVDSVPADEPDLGRDggSRPGRLQGTSSDNQC 741
Ank_5 pfam13857
Ankyrin repeats (many copies);
715-770 6.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 6.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462564264 715 LLACG-ADVNAQDADGATALMCASEYGRLDTVRLLLTqPGCDPAILDNEGTSALAIA 770
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
616-749 1.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSH--GNLAIASLLLDTGaCEVNRQNRAGYSALMLAaltsVRQEEEDMAVVQRLFCMG-DVNAKA 692
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLY----LESNKIDLKILKLLIDKGvDINAKN 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462564264 693 S---------------QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLL 749
Cdd:PHA03100  174 RvnyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_5 pfam13857
Ankyrin repeats (many copies);
687-733 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462564264 687 DVNAKaSQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATAL 733
Cdd:pfam13857   8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
611-771 2.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 611 LLAH--VVNLADGN-GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAaltsVRQEEEDmaVVQRLFCMGD 687
Cdd:PHA02878  153 LLSYgaDINMKDRHkGNTALHYATENKDQRLTELLLSYGA-NVNIPDKTNNSPLHHA----VKHYNKP--IVHILLENGA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 688 VNAKASQTGQTALMLAISHGRQ-DMVATLLACGADVNAQDA-DGATALMCA--SEygrlDTVRLLLtQPGCDPAILDNEG 763
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSikSE----RKLKLLL-EYGADINSLNSYK 300

                  ....*...
gi 2462564264 764 TSALAIAL 771
Cdd:PHA02878  301 LTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
616-763 3.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALTSVrqeeeDMAVVQRLFCMG-DVNAKASQ 694
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTPLHISVGYCK-----DYDILKLLLEHGvDVNAKSYI 267
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462564264 695 TGQTALMLAISHgrQDMVATLLACGADVNAQDADGATAL-MCASEYGRLDTVRLLLTQPGC----DPAILDNEG 763
Cdd:PHA02878  268 LGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILISNICLlkriKPDIKNSEG 339
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
58-586 5.26e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 50.26  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264   58 GPAARRAPGPPTS--RRPRAPRPGLAGARSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLR 135
Cdd:COG3321    854 PGRGRRRVPLPTYpfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  136 ETSRRLELAQTHERAPSPGRGVPRSPRGSGRSSPAPNLAPASPGPAQLQLVREQMAAALRRLRELEDQARTLPELQEQVR 215
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  216 ALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASPRADSPDGLAAGRSEGALQVLYGEVGSLD 295
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  296 GTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGLPAAAERELELLRASLEHQRGVSELLRGR 375
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  376 LRELEEAREAAEEAAAGARAQLREATTQTPWSCAEKAAQTESPAEAPSLTQESSPGSMDGDRAVAPAGILKSIMKKRDGT 455
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264  456 PGAQPSSGPKSLQFVGVLNGEYESSSSEDTSDSDGDSENGGAEPPGSSSGSGDDSGGGSDSGTPGPPSGGDIRDPEPEAE 535
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAAL 1333
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462564264  536 AEPQQVAQGRCELSPRLREACVALQRQLSRPRGVASDGGAVRLVAQEWFRV 586
Cdd:COG3321   1334 AAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
696-726 6.80e-06

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: 43.43  E-value: 6.80e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462564264 696 GQTALMLAISH-GRQDMVATLLACGADVNAQD 726
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
610-654 8.13e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 8.13e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462564264 610 ELLAHVVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQN 654
Cdd:pfam12796  48 LLLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGA-DINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
627-782 8.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 627 LHYSVSHGNLAIASLLLDTGACE-------------------------------------VNRQNRAGYSALMLAALTSV 669
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADInsstknnstplhylsnikynltdvkeivkllleyganVNAPDNNGITPLLYAISKKS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 670 rqeeEDMAVVQRLFCMG-DVNAKASqTGQTALMLAISHGRQD--MVATLLACGADVNAQ----------------DADGA 730
Cdd:PHA03100  119 ----NSYSIVEYLLDNGaNVNIKNS-DGENLLHLYLESNKIDlkILKLLIDKGVDINAKnrvnyllsygvpinikDVYGF 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462564264 731 TALMCASEYGRLDTVRLLLTQpGCDPAILDNEGTSALAIALEAEQDEVAALL 782
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
733-785 2.50e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462564264 733 LMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQDEVAALLHAH 785
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PHA02874 PHA02874
ankyrin repeat protein; Provisional
616-782 6.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 616 VNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALmlaaLTSVRQEEEDMAvvqRLFCMGDVNAKasqt 695
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGA-DINHINTKIPHPL----LTAIKIGAHDII---KLLIDNGVDTS---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 696 gqtalMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIALEAEQ 775
Cdd:PHA02874   96 -----ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNF 169

                  ....*..
gi 2462564264 776 DEVAALL 782
Cdd:PHA02874  170 FDIIKLL 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
622-759 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 622 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAALtsvrqeeedmavvqrlfcMGDVNA-------KASQ 694
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGA-DPDIPNTDKFSPLHLAVM------------------MGDIKGiellidhKACL 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462564264 695 T-----GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMC-ASEYGRLDTVRLLLTQpGCDPAIL 759
Cdd:PHA02875  162 DiedccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADCNIM 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
696-755 1.03e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 696 GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPGCD 755
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
611-728 1.04e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 611 LLAHV--VNLADGNGNTALHYSVSHGNLAIASLLLDtgaCEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-D 687
Cdd:PLN03192  577 LLKHAcnVHIRDANGNTALWNAISAKHHKIFRILYH---FASISDPHAAGDLLCTAA------KRNDLTAMKELLKQGlN 647
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462564264 688 VNAKASQtGQTALMLAISHGRQDMVATLLACGADVNAQDAD 728
Cdd:PLN03192  648 VDSEDHQ-GATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02874 PHA02874
ankyrin repeat protein; Provisional
642-750 1.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 642 LLDTGAcEVNRQNRAGYSALMLAAltsvrqEEEDMAVVQRLFCMG-DVNAKaSQTGQTALMLAISHGRQDMVATLLACGA 720
Cdd:PHA02874  110 ILDCGI-DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                          90       100       110
                  ....*....|....*....|....*....|
gi 2462564264 721 DVNAQDADGATALMCASEYGRLDTVRLLLT 750
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA02876 PHA02876
ankyrin repeat protein; Provisional
670-806 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 670 RQEEEDMAVVQRLFCMG-DVNAKASQTgQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRll 748
Cdd:PHA02876  152 RIQQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK-- 228
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462564264 749 ltqpgcdpAILDNEGTS-----ALAIALEAEQDEVAALLH-AHLSSGQPDTQSESPPGSQTATP 806
Cdd:PHA02876  229 --------AIIDNRSNInkndlSLLKAIRNEDLETSLLLYdAGFSVNSIDDCKNTPLHHASQAP 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
623-666 1.86e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2462564264 623 GNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLAAL 666
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAAS 43
PHA03095 PHA03095
ankyrin-like protein; Provisional
619-752 2.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 619 ADGNGNTALHY--SVSHGNLAIASLLLDTGaCEVNRQNRAGYSAL-MLAALTSVRQeeedmAVVQRLFCMG-DVNAKaSQ 694
Cdd:PHA03095  183 VDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLhSMATGSSCKR-----SLVLPLLIAGiSINAR-NR 255
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462564264 695 TGQTALMLAISHGRQDMVATLLACGADVNAQDADGAT--ALMCASEYGRLdtVRLLL-TQP 752
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTplSLMVRNNNGRA--VRAALaKNP 314
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
622-647 2.25e-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: 39.11  E-value: 2.25e-04
                           10        20
                   ....*....|....*....|....*.
gi 2462564264  622 NGNTALHYSVSHGNLAIASLLLDTGA 647
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
622-655 2.65e-04

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: 38.81  E-value: 2.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462564264 622 NGNTALHYSVSH-GNLAIASLLLDTGAcEVNRQNR 655
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
616-643 3.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.13e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462564264 616 VNLADGNGNTALHYSVSHGNLAIASLLL 643
Cdd:pfam13637  27 INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
623-778 4.79e-04

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: 43.85  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 623 GNTALHYSVSHGNLAIASLLLDTGACEVNR----QNRAGYSALMLAALTsvrqeeEDMAVVQRLFCMG-DV-NAKASQT- 695
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN------QNLNLVRELIARGaDVvSPRATGTf 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 696 -----------GQTALMLAISHGRQDMVATLLACGADVNAQDADGATALmcaseygrldtvRLLLTQPGCDPA--ILDne 762
Cdd:cd22192   125 frpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL------------HILVLQPNKTFAcqMYD-- 190
                         170
                  ....*....|....*.
gi 2462564264 763 gtsaLAIALEAEQDEV 778
Cdd:cd22192   191 ----LILSYDKEDDLQ 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
611-664 7.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 7.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462564264 611 LLAHV---VNLADGNGNTALHYSVSHGNLAIASLLLDTGaCEVNRQNRAGYSALMLA 664
Cdd:pfam13857   1 LLEHGpidLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
696-724 8.74e-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: 37.18  E-value: 8.74e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462564264  696 GQTALMLAISHGRQDMVATLLACGADVNA 724
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
622-798 9.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 622 NGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALMLA----------------ALTSVRQ-----------EEE 674
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAmkfrdseaikllmkhgAIPDVKYpdieselhdavEEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 675 DMAVVQRLFCMGD-VNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYGRLDTVRLLLTQPG 753
Cdd:PHA02875   80 DVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462564264 754 CdPAILDNEGTSALAIALEAEQDEVAALLhahLSSG-QPDTQSESP 798
Cdd:PHA02875  160 C-LDIEDCCGCTPLIIAMAKGDIAICKML---LDSGaNIDYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
670-749 1.54e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 670 RQEEEDMAVVQRLFCMG-DVNAKAS--QTGQTALMLAISHGRQDMVATLLACGADVNAQDADGATALMCASEYG-RLDTV 745
Cdd:PHA03095   21 NASNVTVEEVRRLLAAGaDVNFRGEygKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVI 100

                  ....
gi 2462564264 746 RLLL 749
Cdd:PHA03095  101 KLLI 104
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
696-724 1.61e-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: 36.47  E-value: 1.61e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462564264 696 GQTALMLAISHGRQDMVATLLACGADVNA 724
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
188-409 2.44e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 41.15  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 188 EQMAAALRRLRELEDQARTLPELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLATSERGGRARASP 267
Cdd:COG0515   259 AELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAA 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 268 RADSPDGLAAGRSEGALQVLYGEVGSLDGTPQTREVAAEAVPETREAGAQAVPETREAGVEAAPETVEADAWVTEALLGL 347
Cdd:COG0515   339 AAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAA 418
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462564264 348 PAAAERELELLRASLEHQRGVSELLRGRLRELEEAREAAEEAAAGARAQLREATTQTPWSCA 409
Cdd:COG0515   419 ALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAAALAAAAAAAALA 480
HpnN TIGR03480
hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing ...
188-287 2.97e-03

hopanoid biosynthesis associated RND transporter like protein HpnN; The genomes containing members of this family share the machinery for the biosynthesis of hopanoid lipids. Furthermore, the genes of this family are usually located proximal to other components of this biological process. The proteins appear to be related to the RND family of export proteins, particularly the hydrophobe/amphiphile efflux-3 (HAE3) family represented by TIGR00921.


Pssm-ID: 274598 [Multi-domain]  Cd Length: 862  Bit Score: 41.14  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 188 EQMAAALRRLRELeDQARTL----PELQEQVRALRAEKARLLAGRAQPEPDGEAETRPDKLAQLRRLTERLatserggrA 263
Cdd:TIGR03480 514 RALTERLEALPEV-DQVVTLpdfvPDDQEAKLALIADLALVLGPTLNPGEADPAPSAEEVAAALRRLAARL--------R 584
                          90       100
                  ....*....|....*....|....
gi 2462564264 264 RASPRADSPDGLAAGRSEGALQVL 287
Cdd:TIGR03480 585 AAAAKSQDPDAAAAGRLAASLDRL 608
PHA02875 PHA02875
ankyrin repeat protein; Provisional
586-670 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 586 VSSQRRSQAEPVARMLEGVRrlGPELLAH---VVNLADGNGNTALHYSVSHGNLAIASLLLDTGAcEVNRQNRAGYSALM 662
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIK--GIELLIDhkaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA-NIDYFGKNGCVAAL 206

                  ....*...
gi 2462564264 663 LAALTSVR 670
Cdd:PHA02875  207 CYAIENNK 214
PHA02878 PHA02878
ankyrin repeat protein; Provisional
598-770 7.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 598 ARMLEGVRrlgpELLA--HVVNLADGNGNTALHYSVSHGN-LAIASLLLDTGACEVNRQ---------NRAGYSALMLaa 665
Cdd:PHA02878   47 ARNLDVVK----SLLTrgHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSINKCSVFYTlvaikdafnNRNVEIFKII-- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264 666 LTSVRQEEEDMAVVQ----------------RLFCMG-DVNAKASQTGQTALMLAISHGRQDMVATLLACGADVNAQDAD 728
Cdd:PHA02878  121 LTNRYKNIQTIDLVYidkkskddiieaeitkLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462564264 729 GATALMCASEYGRLDTVRLLLtQPGCDPAILDNEGTSALAIA 770
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
PHA03247 PHA03247
large tegument protein UL36; Provisional
59-181 9.59e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462564264   59 PAARRAPGPPTSRRPRAPRPGlagarSPGAWTSSESLASDDGGAPGILSQGAPSGLLMQPLSPRAPVRNPRVEHTLRETS 138
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPD-----PHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVG 2693
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462564264  139 RRLELAQTHERAPSP---------GRGVPRSPRGSGRSSPAPNLAPASPGPA 181
Cdd:PHA03247  2694 SLTSLADPPPPPPTPepaphalvsATPLPPGPAAARQASPALPAAPAPPAVP 2745
 
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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