|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1150-1383 |
4.33e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.87 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1150 VALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALW 1229
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1230 LAVKEGHWSVVEHLLQRGALLDEPLGQTRkTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKT 1309
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357681 1310 LIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKL 1383
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1262-1354 |
3.29e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1262 LMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRhhEDHNGRTALDLAAYQGAASLVI 1341
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 21357681 1342 YILEQGGNLEHID 1354
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1051-1136 |
1.81e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1051 LCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDitQRCALVHAARMGHLSVVK 1130
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
....*.
gi 21357681 1131 YLLACD 1136
Cdd:pfam12796 79 LLLEKG 84
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1025-1383 |
1.38e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.87 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1025 LKVSRLVLLAGASPNHRtDYMGGAPILcIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGS 1104
Cdd:PHA02876 158 LLIAEMLLEGGADVNAK-DIYCITPIH-YAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1105 SLGQLDITqrcaLVHAARMGHLSVVkyLLACDWSPRPHSQDVTRSVALQQAligAAAQAHCKILEDLLdlnetEFDLDVN 1184
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETS--LLLYDAGFSVNSIDDCKNTPLHHA---SQAPSLSRLVPKLL-----ERGADVN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1185 GmEPSSGELALTAAARHGC-IDVVGILLSRGAQIDARNRQGYSALWLAVK-EGHWSVVEHLLQRGALLDePLGQTRKTPL 1262
Cdd:PHA02876 302 A-KNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN-ARDYCDKTPI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1263 MIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWA-CLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVI 1341
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVI 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21357681 1342 -YILEQGGNLEHIDVHGMRPLDRAIACRNIqaVQVFLRKGAKL 1383
Cdd:PHA02876 460 eMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1277-1516 |
4.03e-08 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 58.08 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1277 LLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVH 1356
Cdd:COG3914 1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1357 GMRPLDRAIACRNIQAVQVFLRKGAKLGPTtwsmamgkpeiLVILLNKLledGNVLYRKNRFQEAAHRYQyalrkisgle 1436
Cdd:COG3914 81 LELAALLLQALGRYEEALALYRRALALNPD-----------NAEALFNL---GNLLLALGRLEEALAALR---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1437 QLLERNAIFAQLrtnlLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQ 1516
Cdd:COG3914 137 RALALNPDFAEA----YLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPD 212
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1029-1099 |
1.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 1.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357681 1029 RLVLLAGASPNHRtDYMGGAPiLCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPL 1099
Cdd:PTZ00322 99 RILLTGGADPNCR-DYDGRTP-LHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1192-1387 |
7.17e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1192 ELALTAAARHGCIDVVGILL-SRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLqRGA--LLDEP------LGQTrktPL 1262
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM-EAApeLVNEPmtsdlyQGET---AL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1263 MIAAEEGHLELVDLLLARGAQ-----------REAQD---HEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTAL 1328
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADvvspratgtffRPGPKnliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1329 DLAAYQGAASLV------IYILEQGGN---LEHIDVH-GMRPLDRAIACRNIQAVQVFLRKGAK----LGPTT 1387
Cdd:cd22192 174 HILVLQPNKTFAcqmydlILSYDKEDDlqpLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQKRRHiqwtYGPLT 246
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1417-1533 |
1.22e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1417 RFQEAAHRYQYALRKISGLEQLLERNAIFAQLR--------------TNLLLNLSRCKRKLNELDASIDLATQAIAQkph 1482
Cdd:pfam07111 430 RIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRqescpppppappvdADLSLELEQLREERNRLDAELQLSAHLIQQ--- 506
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1483 syEGYYARAKARMELGALNEALVDANEAMQQAAQSGV-LCEVVEVLKRIQTE 1533
Cdd:pfam07111 507 --EVGRAREQGEAERQQLSEVAQQLEQELQRAQESLAsVGQQLEVARQGQQE 556
|
|
| PLN03088 |
PLN03088 |
SGT1, suppressor of G2 allele of SKP1; Provisional |
1467-1512 |
2.40e-04 |
|
SGT1, suppressor of G2 allele of SKP1; Provisional
Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 45.16 E-value: 2.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 21357681 1467 DASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQ 1512
Cdd:PLN03088 19 ALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIE 64
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1139-1351 |
6.11e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 44.69 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1139 PRPHSQDVTRSVAlQQALIGAAAQAHCKILEDLLDLNETEfdldvngmePSSGElALTAAARHGCIDVVGILLSRGAQID 1218
Cdd:TIGR00870 40 PKKLNINCPDRLG-RSALFVAAIENENLELTELLLNLSCR---------GAVGD-TLLHAISLEYVDAVEAILLHLLAAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1219 arnRQGYSaLWLAVKEghwsvvehllqrgALLDEPLGQTrktPLMIAAEEGHLELVDLLLARGAQREAQDHEGFtalswa 1298
Cdd:TIGR00870 109 ---RKSGP-LELANDQ-------------YTSEFTPGIT---ALHLAAHRQNYEIVKLLLERGASVPARACGDF------ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1299 CLRGHlaaaktliEHGCNRHhedhnGRTALDLAAYQGAASLVIYILEQGGNLE 1351
Cdd:TIGR00870 163 FVKSQ--------GVDSFYH-----GESPLNAAACLGSPSIVALLSEDPADIL 202
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
1404-1506 |
9.93e-04 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 43.82 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1404 KLLEDGNVLYRKNRFQEAAHRYQYALrkisgleqLLERNAIFAQlrtnlllNLSRCKRKLNELDASIDLATQAIAQKPHS 1483
Cdd:TIGR00990 129 KLKEKGNKAYRNKDFNKAIKLYSKAI--------ECKPDPVYYS-------NRAACHNALGDWEKVVEDTTAALELDPDY 193
|
90 100
....*....|....*....|...
gi 21357681 1484 YEGYYARAKARMELGALNEALVD 1506
Cdd:TIGR00990 194 SKALNRRANAYDGLGKYADALLD 216
|
|
| zf-RING_5 |
pfam14634 |
zinc-RING finger domain; |
97-134 |
4.21e-03 |
|
zinc-RING finger domain;
Pssm-ID: 434085 [Multi-domain] Cd Length: 43 Bit Score: 36.64 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 21357681 97 CPSCRISFDKGKRRKLIdTCGH---ERCYSCMFRNDQCPMC 134
Cdd:pfam14634 2 CNKCFKELSKTRPFYLT-SCGHifcEECLTRLLQERQCPIC 41
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1259-1282 |
5.41e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 5.41e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1150-1383 |
4.33e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 150.87 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1150 VALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALW 1229
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1230 LAVKEGHWSVVEHLLQRGALLDEPLGQTRkTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKT 1309
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357681 1310 LIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKL 1383
Cdd:COG0666 172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1171-1452 |
2.56e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1171 LLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALL 1250
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1251 DEPlGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDL 1330
Cdd:COG0666 81 NAK-DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1331 AAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGA------KLGPTTWSMA--MGKPEILVILL 1402
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAdvnakdNDGKTALDLAaeNGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 21357681 1403 NKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNL 1452
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
979-1295 |
3.75e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 125.07 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 979 MLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPiLCIAAHEG 1058
Cdd:COG0666 20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL-LHAAARNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1059 ILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACdws 1138
Cdd:COG0666 99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1139 prphsqdvtrsvalqqaliGAaaqahckiledlldlnetefdlDVNgMEPSSGELALTAAARHGCIDVVGILLSRGAQID 1218
Cdd:COG0666 176 -------------------GA----------------------DVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357681 1219 ARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLgQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTAL 1295
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD-KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1262-1354 |
3.29e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1262 LMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRhhEDHNGRTALDLAAYQGAASLVI 1341
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 21357681 1342 YILEQGGNLEHID 1354
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1051-1136 |
1.81e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1051 LCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDitQRCALVHAARMGHLSVVK 1130
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
|
....*.
gi 21357681 1131 YLLACD 1136
Cdd:pfam12796 79 LLLEKG 84
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1195-1288 |
3.21e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1195 LTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGqtrKTPLMIAAEEGHLELV 1274
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAARSGHLEIV 77
|
90
....*....|....
gi 21357681 1275 DLLLARGAQREAQD 1288
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1025-1383 |
1.38e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 75.87 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1025 LKVSRLVLLAGASPNHRtDYMGGAPILcIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGS 1104
Cdd:PHA02876 158 LLIAEMLLEGGADVNAK-DIYCITPIH-YAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1105 SLGQLDITqrcaLVHAARMGHLSVVkyLLACDWSPRPHSQDVTRSVALQQAligAAAQAHCKILEDLLdlnetEFDLDVN 1184
Cdd:PHA02876 236 NINKNDLS----LLKAIRNEDLETS--LLLYDAGFSVNSIDDCKNTPLHHA---SQAPSLSRLVPKLL-----ERGADVN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1185 GmEPSSGELALTAAARHGC-IDVVGILLSRGAQIDARNRQGYSALWLAVK-EGHWSVVEHLLQRGALLDePLGQTRKTPL 1262
Cdd:PHA02876 302 A-KNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN-ARDYCDKTPI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1263 MIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWA-CLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVI 1341
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVI 459
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 21357681 1342 -YILEQGGNLEHIDVHGMRPLDRAIACRNIqaVQVFLRKGAKL 1383
Cdd:PHA02876 460 eMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1153-1381 |
6.74e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 72.72 E-value: 6.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1153 QQALIGAAAQAHCKILEDLLDLN-ETEFDLdVNGMEPssgelaLTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLA 1231
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGiNPNFEI-YDGISP------IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1232 VKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLI 1311
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357681 1312 EHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNlehIDVHGMRPlDRAIACRNIQ-----AVQVFLRKGA 1381
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNG-CVAALCYAIEnnkidIVRLFIKRGA 226
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1017-1248 |
8.31e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 69.67 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1017 LRNVYSPNLKVSRLVLLAGASPNHRTDYmGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPL--ILAAMRGHCD 1094
Cdd:PHA03095 55 LHYSSEKVKDIVRLLLEAGADVNAPERC-GFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1095 VVRPLVAAGSSLGQLDITQRCALvhAARMGH----LSVVKYLLACDWSPrpHSQDVTRSVALQQALIGAAAQAhcKILED 1170
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPL--AVLLKSrnanVELLRLLIDAGADV--YAVDDRFRSLLHHHLQSFKPRA--RIVRE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1171 LLDLNETEFDLDVNGMEPssgelaLTAAARHG-CID-VVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGA 1248
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTP------LHSMATGSsCKRsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1084-1221 |
9.10e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 9.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1084 LILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACdwsprphsqdvtrsvalqqaligaaaqa 1163
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 21357681 1164 hckiledlldlnetefdldVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARN 1221
Cdd:pfam12796 53 -------------------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1156-1356 |
1.63e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 66.04 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1156 LIGAAAQAHCKILEDLLdlnETEFDLDVNGmepSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEG 1235
Cdd:PLN03192 529 LLTVASTGNAALLEELL---KAKLDPDIGD---SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1236 HWSVVEHLLQRGALLDEplgqtrktplmiaaeeghlelvdlllargaqreaqdHEGFTALSWACLRGHLAAAKTLIEHGC 1315
Cdd:PLN03192 603 HHKIFRILYHFASISDP------------------------------------HAAGDLLCTAAKRNDLTAMKELLKQGL 646
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21357681 1316 NRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVH 1356
Cdd:PLN03192 647 NVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1198-1381 |
4.33e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.45 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1198 AARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGH-----WSVVEHLLQRGALLDEPlGQTRKTPLMIAAEE--GH 1270
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAP-DNNGITPLLYAISKksNS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1271 LELVDLLLARGAQREAQDHEGFTALSWA--CLRGHLAAAKTLIEHG-----CNR-----------HHEDHNGRTALDLAA 1332
Cdd:PHA03100 121 YSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGvdinaKNRvnyllsygvpiNIKDVYGFTPLHYAV 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21357681 1333 YQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGA 1381
Cdd:PHA03100 201 YNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1054-1263 |
6.23e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1054 AAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLL 1133
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1134 AcdwsprpHSQDVTRS-----VALQQALIgaaaqaHCKILEDLLDLNETEFDLDVNGMEPssgelaLTAAARHGC-IDVV 1207
Cdd:PHA02874 211 D-------HGNHIMNKckngfTPLHNAII------HNRSAIELLINNASINDQDIDGSTP------LHHAINPPCdIDII 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21357681 1208 GILLSRGAQIDARNRQGYSALWLAVKE-GHWSVVEHLLQRGALLDEpLGQTRKTPLM 1263
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKE-ADKLKDSDFL 327
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1066-1270 |
1.42e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.50 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1066 LLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSqd 1145
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA-- 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1146 vtrsvalqqaligaaaqahckiledlldlnetefdldvngmepsSGELaLTAAARHGCIDVVGILLSRGAQIDARNRQGY 1225
Cdd:PLN03192 622 --------------------------------------------AGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21357681 1226 SALWLAVKEGHWSVVEHLLQRGAL-----LDEPLGQTRKTPLMIAAEEGH 1270
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLLIMNGADvdkanTDDDFSPTELRELLQKRELGH 706
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1182-1387 |
1.61e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.88 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1182 DVNGMEpSSGELALTAAARHGC-IDVVGILLSRGAQIDARNRQGYSAL--WLAVKEGHWSVVEHLLQRGALLDEpLGQTR 1258
Cdd:PHA03095 75 DVNAPE-RCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNA-LDLYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1259 KTPLMIAAEEGH--LELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAA--KTLIEHGCNRHHEDHNGRTALDLAAYQ 1334
Cdd:PHA03095 153 MTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATG 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21357681 1335 G--AASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTT 1387
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1260-1311 |
2.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 2.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1260 TPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLI 1311
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1205-1365 |
3.76e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.67 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1205 DVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGAllDEPLGQTRKT-PLMIAAEEGHLELVDLLLARGAQ 1283
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA--DVNIEDDNGCyPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1284 REAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAAslVIYILEQGGNLEHIDVHGMRPLDR 1363
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHH 260
|
..
gi 21357681 1364 AI 1365
Cdd:PHA02874 261 AI 262
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
1277-1516 |
4.03e-08 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 58.08 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1277 LLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVH 1356
Cdd:COG3914 1 AAAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1357 GMRPLDRAIACRNIQAVQVFLRKGAKLGPTtwsmamgkpeiLVILLNKLledGNVLYRKNRFQEAAHRYQyalrkisgle 1436
Cdd:COG3914 81 LELAALLLQALGRYEEALALYRRALALNPD-----------NAEALFNL---GNLLLALGRLEEALAALR---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1437 QLLERNAIFAQLrtnlLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQ 1516
Cdd:COG3914 137 RALALNPDFAEA----YLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPD 212
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1018-1379 |
5.09e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.34 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1018 RNVYSPNLKVSRLVLL--AGASPNHRTDYmgGAPILCIAAHEGILP---MVSLLLEFGADVGLTNSQGCTPLILAAMRGH 1092
Cdd:PHA03095 18 YLLNASNVTVEEVRRLlaAGADVNFRGEY--GKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1093 C-DVVRPLVAAGSSLGQLDITQRCAL-VHAARMG-HLSVVKYLLAcdwsprphsqdvtrsvalqqalIGAaaqahckile 1169
Cdd:PHA03095 96 TlDVIKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLR----------------------KGA---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1170 dllDLNetefDLDVNGMEPssgeLALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALwlavkeghwsvvEHLLQrgal 1249
Cdd:PHA03095 144 ---DVN----ALDLYGMTP----LAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLL------------HHHLQ---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1250 ldeplgQTRKTPlmiaaeeghlELVDLLLARGAQREAQDHEGFTALSWA-----CLRGHLAaakTLIEHGCNRHHEDHNG 1324
Cdd:PHA03095 197 ------SFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRSLVL---PLLIAGISINARNRYG 257
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 21357681 1325 RTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRK 1379
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1020-1110 |
9.27e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1020 VYSPNLKVSRLVLLAGASPNHRTDYmgGAPILCIAAHEGILPMVSLLLEFgADVGLTNsQGCTPLILAAMRGHCDVVRPL 1099
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKN--GRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
|
90
....*....|.
gi 21357681 1100 VAAGSSLGQLD 1110
Cdd:pfam12796 81 LEKGADINVKD 91
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1029-1099 |
1.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 1.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21357681 1029 RLVLLAGASPNHRtDYMGGAPiLCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPL 1099
Cdd:PTZ00322 99 RILLTGGADPNCR-DYDGRTP-LHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1409-1512 |
4.51e-07 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 52.70 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1409 GNVLYRKNRFQEAAHRYQYALRkisgleqlLERNAIFAqlrtnlLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYY 1488
Cdd:COG0457 15 GLAYRRLGRYEEAIEDYEKALE--------LDPDDAEA------LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALN 80
|
90 100
....*....|....*....|....
gi 21357681 1489 ARAKARMELGALNEALVDANEAMQ 1512
Cdd:COG0457 81 NLGLALQALGRYEEALEDYDKALE 104
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1049-1097 |
1.18e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 1.18e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 21357681 1049 PILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVR 1097
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1235-1381 |
2.52e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1235 GHWSVVEHLLQRGalLDEPLGQTR-KTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLieH 1313
Cdd:PLN03192 536 GNAALLEELLKAK--LDPDIGDSKgRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL--Y 611
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357681 1314 GCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGA 1381
Cdd:PLN03192 612 HFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1409-1512 |
2.61e-06 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 50.39 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1409 GNVLYRKNRFQEAahryqyalrkISGLEQLLERNAIFAQLrtnlLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYY 1488
Cdd:COG0457 49 GLAYLRLGRYEEA----------LADYEQALELDPDDAEA----LNNLGLALQALGRYEEALEDYDKALELDPDDAEALY 114
|
90 100
....*....|....*....|....
gi 21357681 1489 ARAKARMELGALNEALVDANEAMQ 1512
Cdd:COG0457 115 NLGLALLELGRYDEAIEAYERALE 138
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1194-1244 |
2.96e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 21357681 1194 ALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLL 1244
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1293-1344 |
4.69e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 4.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1293 TALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYIL 1344
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1073-1331 |
4.83e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 51.12 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1073 VGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLL--ACDWS--PRPHSQDVTR 1148
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdnGVDTSilPIPCIEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1149 SVALQQALIGAAAQAHCKIL-------EDLLDLNET-EFDLDVNgMEPSSGELALTAAARHGCIDVVGILLSRGAQIDAR 1220
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFlhyaikkGDLESIKMLfEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1221 NRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRkTPLMIAAEegHLELVDLLLARGAQREAQDHEGFTALSWA-- 1298
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGF-TPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAin 263
|
250 260 270
....*....|....*....|....*....|....*
gi 21357681 1299 --ClrgHLAAAKTLIEHGCNRHHEDHNGRTALDLA 1331
Cdd:PHA02874 264 ppC---DIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1024-1316 |
5.80e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.82 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1024 NLKVSRLVLLAGASPN-HRTDYMGGAPILCIAAH--EGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRghcdvvrplv 1100
Cdd:PHA03100 47 NIDVVKILLDNGADINsSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK---------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1101 aagsslgqlditqrcalvhaaRMGHLSVVKYLLAcdwsprpHSQDVTrsvalqqaligaaaqahckiledlldlnetefd 1180
Cdd:PHA03100 117 ---------------------KSNSYSIVEYLLD-------NGANVN--------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1181 lDVNgmepSSGELALTAAARHGCID--VVGILLSRGAQIDARNRqgysalwlavkeghwsvVEHLLQRGALLDEP--LGQ 1256
Cdd:PHA03100 136 -IKN----SDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKdvYGF 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1257 TrktPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCN 1316
Cdd:PHA03100 194 T---PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1192-1387 |
7.17e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1192 ELALTAAARHGCIDVVGILL-SRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLqRGA--LLDEP------LGQTrktPL 1262
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM-EAApeLVNEPmtsdlyQGET---AL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1263 MIAAEEGHLELVDLLLARGAQ-----------REAQD---HEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTAL 1328
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADvvspratgtffRPGPKnliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1329 DLAAYQGAASLV------IYILEQGGN---LEHIDVH-GMRPLDRAIACRNIQAVQVFLRKGAK----LGPTT 1387
Cdd:cd22192 174 HILVLQPNKTFAcqmydlILSYDKEDDlqpLDLVPNNqGLTPFKLAAKEGNIVMFQHLVQKRRHiqwtYGPLT 246
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1195-1383 |
1.56e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1195 LTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGAlldeplgQTRKTPLMIAAEEghleLV 1274
Cdd:PHA02874 39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV-------DTSILPIPCIEKD----MI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1275 DLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHID 1354
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180
....*....|....*....|....*....
gi 21357681 1355 VHGMRPLDRAIACRNIQAVQVFLRKGAKL 1383
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHI 216
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
1390-1517 |
2.16e-05 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 45.95 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1390 MAMGKPEILVILLNKLLED-----------GNVLYRKNRFQEAAHRYQYALRKisgleqllernaifAQLRTNLLLNLSR 1458
Cdd:COG4783 15 LLAGDYDEAEALLEKALELdpdnpeafallGEILLQLGDLDEAIVLLHEALEL--------------DPDEPEARLNLGL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 21357681 1459 CKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQS 1517
Cdd:COG4783 81 ALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
1394-1510 |
2.81e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.31 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1394 KPEILVILLNKlledGNVLYRKNRFQEAAHRYQYALRkisgleqlLERNAIFAqlrtnlLLNLSRCKRKLNELDASIDLA 1473
Cdd:COG0457 72 DPDDAEALNNL----GLALQALGRYEEALEDYDKALE--------LDPDDAEA------LYNLGLALLELGRYDEAIEAY 133
|
90 100 110
....*....|....*....|....*....|....*..
gi 21357681 1474 TQAIAQKPHSYEGYYARAKARMELGALNEALVDANEA 1510
Cdd:COG0457 134 ERALELDPDDADALYNLGIALEKLGRYEEALELLEKL 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1082-1133 |
5.74e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1082 TPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLL 1133
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1205-1278 |
9.03e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 9.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357681 1205 DVVG--ILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGA---LLDeplgQTRKTPLMIAAEEGHLELVDLLL 1278
Cdd:PTZ00322 94 DAVGarILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdptLLD----KDGKTPLELAEENGFREVVQLLS 168
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1245-1383 |
1.09e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.56 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1245 QRGALLDEPLGQtrktpLMIAAEEGHLELVDLLLARGAQREAQDHEGFTAL-SWACLRGHLAAAKTLIEHGCNRHHEDHN 1323
Cdd:PHA03095 42 FRGEYGKTPLHL-----YLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357681 1324 GRTALD--LAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQA--VQVFLRKGAKL 1383
Cdd:PHA03095 117 GRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADV 180
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1417-1533 |
1.22e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1417 RFQEAAHRYQYALRKISGLEQLLERNAIFAQLR--------------TNLLLNLSRCKRKLNELDASIDLATQAIAQkph 1482
Cdd:pfam07111 430 RIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRqescpppppappvdADLSLELEQLREERNRLDAELQLSAHLIQQ--- 506
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1483 syEGYYARAKARMELGALNEALVDANEAMQQAAQSGV-LCEVVEVLKRIQTE 1533
Cdd:pfam07111 507 --EVGRAREQGEAERQQLSEVAQQLEQELQRAQESLAsVGQQLEVARQGQQE 556
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1039-1334 |
1.44e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.41 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1039 NHRTDYMGGAP-ILCIAAHEGI----LPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVaagSSLGQLDITQ 1113
Cdd:PHA02878 24 DHTENYSTSASlIPFIPLHQAVearnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1114 rcALVHAARMGH---LSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAaaqahcKILEDLLdlnetEFDLDVNGMEPSS 1190
Cdd:PHA02878 101 --TLVAIKDAFNnrnVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEA------EITKLLL-----SYGADINMKDRHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1191 GELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEpLGQTRKTPLMIAAeeGH 1270
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA-RDKCGNTPLHISV--GY 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1271 L---ELVDLLLARGAQREAQDH-EGFTALswaclrgHLA-----AAKTLIEHGCNRHHEDHNGRTALDLAAYQ 1334
Cdd:PHA02878 245 CkdyDILKLLLEHGVDVNAKSYiLGLTAL-------HSSikserKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PLN03088 |
PLN03088 |
SGT1, suppressor of G2 allele of SKP1; Provisional |
1467-1512 |
2.40e-04 |
|
SGT1, suppressor of G2 allele of SKP1; Provisional
Pssm-ID: 215568 [Multi-domain] Cd Length: 356 Bit Score: 45.16 E-value: 2.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 21357681 1467 DASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQ 1512
Cdd:PLN03088 19 ALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIE 64
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1263-1340 |
2.64e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1263 MIAAEEGHLEL------VDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGA 1336
Cdd:PTZ00322 81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
....
gi 21357681 1337 ASLV 1340
Cdd:PTZ00322 161 REVV 164
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1040-1106 |
3.19e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 45.63 E-value: 3.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357681 1040 HRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSL 1106
Cdd:PLN03192 615 SISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1277-1331 |
5.10e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 5.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21357681 1277 LLARGAQR-EAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLA 1331
Cdd:pfam13857 1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1139-1351 |
6.11e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 44.69 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1139 PRPHSQDVTRSVAlQQALIGAAAQAHCKILEDLLDLNETEfdldvngmePSSGElALTAAARHGCIDVVGILLSRGAQID 1218
Cdd:TIGR00870 40 PKKLNINCPDRLG-RSALFVAAIENENLELTELLLNLSCR---------GAVGD-TLLHAISLEYVDAVEAILLHLLAAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1219 arnRQGYSaLWLAVKEghwsvvehllqrgALLDEPLGQTrktPLMIAAEEGHLELVDLLLARGAQREAQDHEGFtalswa 1298
Cdd:TIGR00870 109 ---RKSGP-LELANDQ-------------YTSEFTPGIT---ALHLAAHRQNYEIVKLLLERGASVPARACGDF------ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1299 CLRGHlaaaktliEHGCNRHhedhnGRTALDLAAYQGAASLVIYILEQGGNLE 1351
Cdd:TIGR00870 163 FVKSQ--------GVDSFYH-----GESPLNAAACLGSPSIVALLSEDPADIL 202
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
1409-1504 |
6.27e-04 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 41.53 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1409 GNVLYRKNRFQEAAHRYQYALRkisgleqLLERNAifaqlrtNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYY 1488
Cdd:COG4235 24 GRAYLRLGRYDEALAAYEKALR-------LDPDNA-------DALLDLAEALLAAGDTEEAEELLERALALDPDNPEALY 89
|
90
....*....|....*.
gi 21357681 1489 ARAKARMELGALNEAL 1504
Cdd:COG4235 90 LLGLAAFQQGDYAEAI 105
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
1411-1515 |
8.19e-04 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 40.15 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1411 VLYRKNRFQEAAHRYQYALRkisgleqlLERNAIFAqlrtnlLLNLSRCKRKLNELDASIDLaTQAIAQKPHSYEGYYAR 1490
Cdd:COG3063 1 LYLKLGDLEEAEEYYEKALE--------LDPDNADA------LNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNL 65
|
90 100
....*....|....*....|....*
gi 21357681 1491 AKARMELGALNEALVDANEAMQQAA 1515
Cdd:COG3063 66 AELLLELGDYDEALAYLERALELDP 90
|
|
| 3a0801s09 |
TIGR00990 |
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ... |
1404-1506 |
9.93e-04 |
|
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 273380 [Multi-domain] Cd Length: 615 Bit Score: 43.82 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1404 KLLEDGNVLYRKNRFQEAAHRYQYALrkisgleqLLERNAIFAQlrtnlllNLSRCKRKLNELDASIDLATQAIAQKPHS 1483
Cdd:TIGR00990 129 KLKEKGNKAYRNKDFNKAIKLYSKAI--------ECKPDPVYYS-------NRAACHNALGDWEKVVEDTTAALELDPDY 193
|
90 100
....*....|....*....|...
gi 21357681 1484 YEGYYARAKARMELGALNEALVD 1506
Cdd:TIGR00990 194 SKALNRRANAYDGLGKYADALLD 216
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1191-1295 |
1.71e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1191 GELALTAAARHGCIDVVGILLsRGA------QIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPlgqtRKT---- 1260
Cdd:cd22192 51 GETALHVAALYDNLEAAVVLM-EAApelvnePMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtff 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 21357681 1261 -------------PLMIAAEEGHLELVDLLLARGAQREAQDHEGFTAL 1295
Cdd:cd22192 126 rpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1243-1295 |
1.85e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 21357681 1243 LLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTAL 1295
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1032-1087 |
1.93e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21357681 1032 LLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILA 1087
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1051-1135 |
2.88e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1051 LCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVK 1130
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*
gi 21357681 1131 YLLAC 1135
Cdd:PTZ00322 166 LLSRH 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1224-1278 |
2.88e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 21357681 1224 GYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRkTPLMIAAEEGHLELVDLLL 1278
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASNGNVEVLKLLL 54
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1390-1517 |
3.14e-03 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 41.25 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1390 MAMGKPEILVILLNKLLE----DGNVLYRKNRFQEAAHRYQYALRKisgLEQLLERNAIFAQLrtnlLLNLSRCKRKLNE 1465
Cdd:COG2956 87 LKAGLLDRAEELLEKLLEldpdDAEALRLLAEIYEQEGDWEKAIEV---LERLLKLGPENAHA----YCELAELYLEQGD 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 21357681 1466 LDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQS 1517
Cdd:COG2956 160 YDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211
|
|
| zf-RING_5 |
pfam14634 |
zinc-RING finger domain; |
97-134 |
4.21e-03 |
|
zinc-RING finger domain;
Pssm-ID: 434085 [Multi-domain] Cd Length: 43 Bit Score: 36.64 E-value: 4.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 21357681 97 CPSCRISFDKGKRRKLIdTCGH---ERCYSCMFRNDQCPMC 134
Cdd:pfam14634 2 CNKCFKELSKTRPFYLT-SCGHifcEECLTRLLQERQCPIC 41
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1310-1364 |
4.82e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 4.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21357681 1310 LIEHGCNRH-HEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRA 1364
Cdd:pfam13857 1 LLEHGPIDLnRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| zf-C3HC4 |
pfam00097 |
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ... |
97-134 |
5.12e-03 |
|
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.
Pssm-ID: 395049 [Multi-domain] Cd Length: 40 Bit Score: 36.18 E-value: 5.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 21357681 97 CPSCrisFDKGKRRKLIDTCGHERCYSCMFR-----NDQCPMC 134
Cdd:pfam00097 1 CPIC---LEEPKDPVTLLPCGHLFCSKCIRSwlesgNVTCPLC 40
|
|
| TadD |
COG5010 |
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ... |
1398-1517 |
5.28e-03 |
|
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 39.17 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1398 LVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAI 1477
Cdd:COG5010 2 RALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 21357681 1478 AQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQS 1517
Cdd:COG5010 82 QLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDN 121
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1259-1282 |
5.41e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 5.41e-03
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
1405-1531 |
6.79e-03 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 40.10 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1405 LLEDGNVLYRKNRFQEAAHRYQYALRkisgleqlLERNAIFAQLrtnlllNLSRCKRKLNELDASIDLATQAIAQKPHSY 1484
Cdd:COG2956 147 YCELAELYLEQGDYDEAIEALEKALK--------LDPDCARALL------LLAELYLEQGDYEEAIAALERALEQDPDYL 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 21357681 1485 EGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQ 1531
Cdd:COG2956 213 PALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKE 259
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1260-1289 |
7.32e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.73 E-value: 7.32e-03
10 20 30
....*....|....*....|....*....|.
gi 21357681 1260 TPLMIAAEE-GHLELVDLLLARGAQREAQDH 1289
Cdd:pfam00023 4 TPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
1200-1284 |
8.22e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 38.70 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357681 1200 RHG--CIDVVG------------ILLSRGAQIDARNRQ-GYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMI 1264
Cdd:PHA02736 53 RHGkqCVHIVSnpdkadpqeklkLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYV 132
|
90 100
....*....|....*....|
gi 21357681 1265 AAEEGHLELVDLLLARGAQR 1284
Cdd:PHA02736 133 ACERHDAKMMNILRAKGAQC 152
|
|
| |
