|
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
|
| 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
|
| 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
|
|
|