|
Name |
Accession |
Description |
Interval |
E-value |
| parp_like |
cd01437 |
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
2153-2550 |
3.07e-88 |
|
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.
Pssm-ID: 238717 [Multi-domain] Cd Length: 347 Bit Score: 292.25 E-value: 3.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2153 PSKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMPLGRLTRDGIDAAMQIIADLRKLIRevpicaalrgrhsyhddkeg 2232
Cdd:cd01437 1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALK-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2233 eeeenaveeanaeadNGANgegtkkkkkkkeltleemreLYEEIAELSNRFYELIPHaEYTIESIPPLNTNDLLNKKAQp 2312
Cdd:cd01437 61 ---------------RGSS--------------------QGSQLEELSNEFYTLIPH-DFGMSKPPVIDNEELLKAKRE- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2313 shdhtLLSNLAEIRTAAKILLGAHYRVKeiNPLDYCYSAMHIRLSQLPKETDEYKILRQYIKRSSPSVF-----VTNIYH 2387
Cdd:cd01437 104 -----LLEALRDIEIASKLLKDDEDDSD--DPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTHAPTTeytveVQEIFR 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2388 LQRKGEPERFQeRWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCrmgHTGsrh 2467
Cdd:cd01437 177 VEREGETDRFK-PFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMFSKSANYC---HAS--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2468 sqpERKNTGFMLMCEVALGEMNAITQAEYMEK-APQGFHSTKGIGQRGPDPSKTIVVPSGVTIPVGEImqYPKTPGHHYG 2546
Cdd:cd01437 250 ---ASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKP--VPSGHKTDTS 324
|
....
gi 470409102 2547 LQHN 2550
Cdd:cd01437 325 LLYN 328
|
|
| PLN03124 |
PLN03124 |
poly [ADP-ribose] polymerase; Provisional |
1957-2551 |
4.03e-86 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 297.13 E-value: 4.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1957 DWEHDSAELLNNPPEPSDEEKAEQQEKAREKQ------KHAHPVDKNFDQRQNSEVYAENKG-EVYDVTLTTVDVRYGTh 2029
Cdd:PLN03124 112 ALESDVKVGSANGTGEDEKEKGGDEEREKEEKivtatkKGRAVLDQWLPDHIKSNYHVLEEGdDVYDAMLNQTNVGDNN- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2030 giNNFYKMQVIHNKLKDFYILWTRWGRIGDVGQYQ-RTPFPTAEATVEEFKKIFKAKTGNSWEDRANFEKKPKKYHMIKL 2108
Cdd:PLN03124 191 --NKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKlHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEM 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2109 ETNKEKLVANLLKPFDIELEDEaqgggaaadahakplsvasrypPSKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMP 2188
Cdd:PLN03124 269 DYEDEEESKKDKPSVSSEDKNK----------------------QSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2189 LGRLTRDGIDAAMQIiadLRKlirevpICAALrgrhsyhdDKEGEeeenaveeanaeadngangegtkkkkkkkeltlee 2268
Cdd:PLN03124 327 LGKLSKSTILKGYEV---LKR------IAEVI--------SRSDR----------------------------------- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2269 mrelyEEIAELSNRFYELIPH-------AEYTIesipplNTNDLLNKKAQpshdhtLLSNLAEIRTAAKILLGAHYrvKE 2341
Cdd:PLN03124 355 -----ETLEELSGEFYTVIPHdfgfkkmRQFTI------DTPQKLKHKLE------MVEALGEIEIATKLLKDDIG--EQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2342 INPLDYCYSAMHIRLSQLPKETDEYKILRQYIKR------SSPSVFVTNIYHLQRKGEPERFQeRWEKVPNHQLLFHGSA 2415
Cdd:PLN03124 416 DDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENthgqthSGYTLEIVQIFKVSREGEDERFQ-KFSSTKNRMLLWHGSR 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2416 LSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCrmgHTGSrhsqpeRKNTGFMLMCEVALGEMNAITQAE 2495
Cdd:PLN03124 495 LTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYC---YASA------ANPDGVLLLCEVALGDMNELLQAD 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 2496 Y-MEKAPQGFHSTKGIGQRGPDPSKTIVVPSGVTIPVGEIMQYPKTPGhhyGLQHND 2551
Cdd:PLN03124 566 YnANKLPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGKPVESPYSKG---SLEYNE 619
|
|
| PARP |
pfam00644 |
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
2363-2533 |
2.38e-57 |
|
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.
Pssm-ID: 395519 [Multi-domain] Cd Length: 195 Bit Score: 197.56 E-value: 2.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2363 TDEYKILRQYIKRSSPSV-----FVTNIYHLQRKGEPERFQErWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFS 2437
Cdd:pfam00644 1 SEEYQIIEKYFLSTHDPThgyplFILEIFRVQRDGEWERFQP-KKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2438 GYAFGKGIYFADMFQKSFGYCRMGHTgsrhsqperKNTGFMLMCEVALGEMNAITQAEYMEKAPQGFHSTKGIGQRGPDP 2517
Cdd:pfam00644 80 GYMFGKGIYFADDASKSANYCPPSEA---------HGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES 150
|
170
....*....|....*..
gi 470409102 2518 SKTIV-VPSGVTIPVGE 2533
Cdd:pfam00644 151 FVDLDgVPLGKLVATGY 167
|
|
| WGR_PARP |
cd07997 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
2011-2110 |
3.69e-42 |
|
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.
Pssm-ID: 153426 Cd Length: 102 Bit Score: 150.15 E-value: 3.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2011 KGEVYDVTLTTVDVRYGthgINNFYKMQVIHNKLKDFYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSW 2090
Cdd:cd07997 6 IATVYDATLNQTDISNN---NNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEW 82
|
90 100
....*....|....*....|
gi 470409102 2091 EDRANFEKKPKKYHMIKLET 2110
Cdd:cd07997 83 ENRPLFKKQPGKYALVELDY 102
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1228-1508 |
3.39e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 3.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1228 TALHFLVSQPDLLSDFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAM 1307
Cdd:COG0666 23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1308 VDALLQANTDVD-KWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNAS 1386
Cdd:COG0666 103 VKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1387 DNNGSSGLHYAVTYaepgadASFEIEDFLLKKGANVNKRDNHGRVPLHYAfLKTGNQNtpidpietVSSLCAVRDLEIDV 1466
Cdd:COG0666 183 DNDGETPLHLAAEN------GHLEIVKLLLEAGADVNAKDNDGKTALDLA-AENGNLE--------IVKLLLEAGADLNA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 470409102 1467 ADNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPL 1508
Cdd:COG0666 248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
751-982 |
6.85e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 6.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVA 830
Cdd:COG0666 56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 831 LNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLEQPsVDVNI 910
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG-ADVNA 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 911 RDDDGRTLAsqlmDIVCESSHKQLQYLIEKKSADVTTPDTKGLTPLHYVAQNFDPVQAAAEFKADNDNSDAD 982
Cdd:COG0666 215 KDNDGKTAL----DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1250-1569 |
1.01e-28 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 122.83 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1250 DINAQDRKMETPLHLAIN---GDRQDVFNMLLaESSINANVADSLGTLPLHLAV-NRQNLAMVDALLQANTDVDKWQR-G 1324
Cdd:PHA03095 39 DVNFRGEYGKTPLHLYLHyssEKVKDIVRLLL-EAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIKAGADVNAKDKvG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1325 RAALHT--AVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKN--MNLVRILVQAGADVNASDNNGSSGLHYAVTY 1400
Cdd:PHA03095 118 RTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1401 AEPGADASFEiedfLLKKGANVNKRDNHGRVPLHYAFLKTGNQNTPIDP--IETVSslcavrdleIDVADNHKRTPLHYA 1478
Cdd:PHA03095 198 FKPRARIVRE----LIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGIS---------INARNRYGQTPLHYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1479 AQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANVrHPIYNVtwgFAHDENQRHKRVIThsTS 1558
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA-ETVAAT---LNTASVAGGDIPSD--AT 338
|
330
....*....|.
gi 470409102 1559 RSMFYEAVSRG 1569
Cdd:PHA03095 339 RLCVAKVVLRG 349
|
|
| WGR |
smart00773 |
Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
2011-2097 |
5.65e-25 |
|
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.
Pssm-ID: 214814 Cd Length: 84 Bit Score: 100.44 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2011 KGEVYDVTLTTVDvryGTHGINNFYKMQVIHNKLKDfYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSW 2090
Cdd:smart00773 2 GGEIYDVYLNFTD---LASNNNKFYIIQLLEDDFGG-YSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGY 77
|
....*..
gi 470409102 2091 EDRANFE 2097
Cdd:smart00773 78 EERGKFV 84
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1337-1762 |
2.29e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 109.34 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1337 LAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNL---VRILVQAGADVNASDNNGSSGLHYAVTYAEpgadaSFEIED 1413
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAT-----TLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1414 FLLKKGANVNKRDNHGRVPLHyAFLKTGNQNTPIdpIEtvsslcavrdleidvadnhkrtplhyaaqrgattcslLLLNR 1493
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLH-VYLSGFNINPKV--IR-------------------------------------LLLRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1494 KAGLENQDEDGNTPLGLGLKNGHGDYAIV--LLQKNANVrhpiynvtwgFAHDENqrhKRVITHSTSRSmfyeavSRGWQ 1571
Cdd:PHA03095 142 GADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADV----------YAVDDR---FRSLLHHHLQS------FKPRA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1572 GVSYMMLDAGLDkltaltdaintgkfqlvvtllsktpedevVQGLDADDRTLFHHLANYCSGKldhwaQTLAEKLEERGV 1651
Cdd:PHA03095 203 RIVRELIRAGCD-----------------------------PAATDMLGNTPLHSMATGSSCK-----RSLVLPLLIAGI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1652 AMNVIDKHGRLPLHYASKNGCGVLVDFFLKRSkSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKN 1731
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTAS 327
|
410 420 430
....*....|....*....|....*....|....*
gi 470409102 1732 QAHGRHNTPEKKQRRHA----KAAAALSKVAQETH 1762
Cdd:PHA03095 328 VAGGDIPSDATRLCVAKvvlrGAFSLLPEPIRAYH 362
|
|
| WGR |
pfam05406 |
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
2015-2097 |
1.15e-23 |
|
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.
Pssm-ID: 398851 Cd Length: 79 Bit Score: 96.54 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2015 YDVTLTTVDVRYGThgiNNFYKMQvIHNKLKDFYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSWEDRA 2094
Cdd:pfam05406 1 YDLYLEQTDAARNS---NKFYEIQ-VEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERG 76
|
...
gi 470409102 2095 NFE 2097
Cdd:pfam05406 77 EFE 79
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1642-1935 |
8.69e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.10 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1642 LAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADcs 1721
Cdd:COG0666 69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1722 aldarvkqknqahgrhntpekkqrrhakaaaalskvaqethlviyamrasladllnlllankadLNAKDSLGNTCLIYAV 1801
Cdd:COG0666 146 ----------------------------------------------------------------VNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1802 RNNDTDMVHLLftkrrgaakpgpssssssssappsslspaepelmLENetGIDPNVQDEQGKTALHHVVSpldYGSYENV 1881
Cdd:COG0666 162 ANGNLEIVKLL----------------------------------LEA--GADVNARDNDGETPLHLAAE---NGHLEIV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1882 ALLtmlLKAGADPNVKDNQGHTPLYYALQQRDGVMAARLRSLGAKLDKKEEANL 1935
Cdd:COG0666 203 KLL---LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1033-1400 |
4.85e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.81 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1033 VVIAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQIAAIHVQDRNVLHqltpQLMERDLLPLLEAIARN 1112
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE----CAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1113 VGEQRFKEMA-----RELDDEgfTPFLRFVQHYGIWSPDHKAKVP-SRTKQAPPVvnpeerrrqekaardrfRRFLVRFI 1186
Cdd:PHA02876 234 RSNINKNDLSllkaiRNEDLE--TSLLLYDAGFSVNSIDDCKNTPlHHASQAPSL-----------------SRLVPKLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1187 ELGAvDTTApvrstkawRDWKKADPQPKQSPGKYSlTDGRRTalhfLVSQpdllsdfiheyKLDINAQDRKMETPLHLAI 1266
Cdd:PHA02876 295 ERGA-DVNA--------KNIKGETPLYLMAKNGYD-TENIRT----LIML-----------GADVNAADRLYITPLHQAS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1267 NGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKW-QRGRAALHTAVDCCN-LAIINSLL 1344
Cdd:PHA02876 350 TLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsQKIGTALHFALCGTNpYMSVKTLI 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 1345 RAKANVNIQDSQHKTPLHYALQRK-NMNLVRILVQAGADVNASDNNGSSGLHYAVTY 1400
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY 486
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
753-878 |
4.51e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.54 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 753 LHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEagcnieaadklkrtaviHAARNgqlvaln 832
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-----------------HADVN------- 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 470409102 833 yllrmsaaaccADSSTNTAAHYAAAFGWRACLELLVENGADPNAPN 878
Cdd:pfam12796 57 -----------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
740-922 |
3.58e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.84 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 740 YIDTKSKgSRFTALHFAVRNNQPEAV-KLLIEKGAHIEAPDVNRMTPLhHAVALGF---VDVAKELVEAGCNIEAADKLK 815
Cdd:PHA03095 75 DVNAPER-CGFTPLHLYLYNATTLDViKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 816 RTAV-----------------------IHAARNGQLVALNYLL----------RMSAAACC----ADSSTNTAAHYAAAF 858
Cdd:PHA03095 153 MTPLavllksrnanvellrllidagadVYAVDDRFRSLLHHHLqsfkprarivRELIRAGCdpaaTDMLGNTPLHSMATG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470409102 859 GW--RACLELLVENGADPNAPNDWKTTPL---AIALQKGhlACaDFLLEQPSvDVNIRDDDGRTLASQL 922
Cdd:PHA03095 233 SSckRSLVLPLLIAGISINARNRYGQTPLhyaAVFNNPR--AC-RRLIALGA-DINAVSSDGNTPLSLM 297
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1583-1795 |
7.74e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 77.69 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1583 DKLTALTDAINTGKFQLVVTLLSKTPEDEVVqglDADDRTLFHHLANYcsGKLDhwaqtLAEKLEERGVAMNVIDKHGRL 1662
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR---DKDGETPLHLAAYN--GNLE-----IVKLLLEAGADVNAQDNDGNT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1663 PLHYASKNGCGVLVDFFLKRsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKNQAHGRHNTPEK 1742
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1743 KQRRHAKAAAALSKVAQETHLVIYAMRASLADLLNLLLANKADLNAKDSLGNT 1795
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1328-1426 |
9.85e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1328 LHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQaGADVNaSDNNGSSGLHYAVTYaepgadA 1407
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARS------G 72
|
90
....*....|....*....
gi 470409102 1408 SFEIEDFLLKKGANVNKRD 1426
Cdd:pfam12796 73 HLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
681-812 |
5.16e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 681 LMIAAQCGRLDSIKLLLDwdsrkmaeaekeaEESDKEHSSDDDEeeeaprkqpraklvpyidtkskgsrfTALHFAVRNN 760
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE-------------NGADANLQDKNGR--------------------------TALHLAAKNG 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 470409102 761 QPEAVKLLIEKgAHIEAPDvNRMTPLHHAVALGFVDVAKELVEAGCNIEAAD 812
Cdd:pfam12796 42 HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1642-1724 |
1.19e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.35 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1642 LAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKrsKSDVNLIDeNGKSPLVYAVLGSHLQVAERLMARKADCS 1721
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
|
...
gi 470409102 1722 ALD 1724
Cdd:pfam12796 89 VKD 91
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1268-1494 |
1.50e-07 |
|
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: 57.01 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1268 GDRQDVFNMLLAESSINANVADSLGTLPLHLAVNR-QNLAMVDALLQANTDVDKwqrGRAALHTA----VDCCNLAIINS 1342
Cdd:TIGR00870 28 GDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIEnENLELTELLLNLSCRGAV---GDTLLHAIsleyVDAVEAILLHL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1343 LLRAKANVNIQ---DSQ------HKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEPG--------A 1405
Cdd:TIGR00870 105 LAAFRKSGPLElanDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGesplnaaaC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1406 DASFEIEDFLLKKGANVNKRDNHGRVPLHYAFLKTGNQNtpiDPIETVSS-----------LCAVRDLEIDVadNHK-RT 1473
Cdd:TIGR00870 185 LGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKA---EYEELSCQmynfalslldkLRDSKELEVIL--NHQgLT 259
|
250 260
....*....|....*....|.
gi 470409102 1474 PLHYAAQRGATTCSLLLLNRK 1494
Cdd:TIGR00870 260 PLKLAAKEGRIVLFRLKLAIK 280
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1294-1494 |
1.71e-07 |
|
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: 56.56 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1294 LPLHLAVNRQNLAMVDALLQANtDVDKWQRG---RAALHTAVDCCNLAIINSLLRAK---ANVNIQDS--QHKTPLHYAL 1365
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGalgETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1366 QRKNMNLVRILVQAGADVNASDNNGssglhyavTYAEPGADA---------SF-------EIEDFLLKKGANVNKRDNHG 1429
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATG--------TFFRPGPKNliyygehplSFaacvgneEIVRLLIEHGADIRAQDSLG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 1430 RVPLHYAFLKTgNQNTPIDPIETVSSLCA-VRDLEIDVADNHK-RTPLHYAAQRGATTCSLLLLNRK 1494
Cdd:cd22192 170 NTVLHILVLQP-NKTFACQMYDLILSYDKeDDLQPLDLVPNNQgLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1620-1925 |
3.85e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1620 DRTLFHHLANYCSGKLDHWAQTLAEKleerGVAMNVIDKHGRLPLHYASKNGCGV-LVDFFLKRsKSDVNLIDENGKSPL 1698
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDIVRLLLEA----GADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA-GADVNAKDKVGRTPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1699 -VY-AVLGSHLQVAERLMARKADCSALDArvkqknqaHGRhnTPekkqrrhakAAAALSKVAQETHLVIYAMRASladll 1776
Cdd:PHA03095 122 hVYlSGFNINPKVIRLLLRKGADVNALDL--------YGM--TP---------LAVLLKSRNANVELLRLLIDAG----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1777 nlllankADLNAKDSLGNTCLIYavrnndtdmvHLLFTKRRgaakpgpssssssssappsslspaePELMLEN-ETGIDP 1855
Cdd:PHA03095 178 -------ADVYAVDDRFRSLLHH----------HLQSFKPR-------------------------ARIVRELiRAGCDP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1856 NVQDEQGKTALHHvvspLDYGSYENVALLTMLLKAGADPNVKDNQGHTPLYYALQQRDGVMAARLRSLGA 1925
Cdd:PHA03095 216 AATDMLGNTPLHS----MATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1797-1930 |
1.92e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1797 LIYAVRNNDTDMVHLLFtkrrgaakpgpssssssssappsslspaepelmlenETGIDPNVQDEQGKTALHHVVSpldYG 1876
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL------------------------------------ENGADANLQDKNGRTALHLAAK---NG 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1877 SYENValltMLLKAGADPNVKDNqGHTPLYYALQQRDGVMAARLRSLGAKLDKK 1930
Cdd:pfam12796 42 HLEIV----KLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| WGR |
COG3831 |
WGR domain, predicted DNA-binding domain in MolR [Transcription]; |
2034-2086 |
7.35e-05 |
|
WGR domain, predicted DNA-binding domain in MolR [Transcription];
Pssm-ID: 443043 Cd Length: 83 Bit Score: 43.44 E-value: 7.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 2034 FYKMQVIHNKLKDfYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKT 2086
Cdd:COG3831 17 FYELEVEPDLFGG-WSLTRRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKL 68
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1356-1385 |
7.37e-05 |
|
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: 41.80 E-value: 7.37e-05
10 20 30
....*....|....*....|....*....|
gi 470409102 1356 QHKTPLHYALQRKNMNLVRILVQAGADVNA 1385
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1035-1098 |
1.48e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.80 E-value: 1.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQiaaihvqdRNVLHQLTPqLM 1098
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--------NLKDNGRTA-LH 66
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
751-821 |
2.58e-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: 46.54 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPdvnRMT-----------------PLHHAVALGFVDVAKELVEAGCNIEAADK 813
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
|
....*...
gi 470409102 814 LKRTaVIH 821
Cdd:cd22192 168 LGNT-VLH 174
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
725-823 |
4.63e-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: 45.84 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 725 EEEAPRKQPRAKLV--PYIDTKSKGSrfTALHFAVRNNQPEAVKLLIEKGAHIEA----------PDVNRM----TPLHH 788
Cdd:TIGR00870 104 LLAAFRKSGPLELAndQYTSEFTPGI--TALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNA 181
|
90 100 110
....*....|....*....|....*....|....*
gi 470409102 789 AVALGFVDVAKELVEAGCNIEAADKLKRTaVIHAA 823
Cdd:TIGR00870 182 AACLGSPSIVALLSEDPADILTADSLGNT-LLHLL 215
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
750-777 |
4.09e-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: 36.80 E-value: 4.09e-03
10 20
....*....|....*....|....*...
gi 470409102 750 FTALHFAVRNNQPEAVKLLIEKGAHIEA 777
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| parp_like |
cd01437 |
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
2153-2550 |
3.07e-88 |
|
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.
Pssm-ID: 238717 [Multi-domain] Cd Length: 347 Bit Score: 292.25 E-value: 3.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2153 PSKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMPLGRLTRDGIDAAMQIIADLRKLIRevpicaalrgrhsyhddkeg 2232
Cdd:cd01437 1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALK-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2233 eeeenaveeanaeadNGANgegtkkkkkkkeltleemreLYEEIAELSNRFYELIPHaEYTIESIPPLNTNDLLNKKAQp 2312
Cdd:cd01437 61 ---------------RGSS--------------------QGSQLEELSNEFYTLIPH-DFGMSKPPVIDNEELLKAKRE- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2313 shdhtLLSNLAEIRTAAKILLGAHYRVKeiNPLDYCYSAMHIRLSQLPKETDEYKILRQYIKRSSPSVF-----VTNIYH 2387
Cdd:cd01437 104 -----LLEALRDIEIASKLLKDDEDDSD--DPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNTHAPTTeytveVQEIFR 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2388 LQRKGEPERFQeRWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCrmgHTGsrh 2467
Cdd:cd01437 177 VEREGETDRFK-PFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMFSKSANYC---HAS--- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2468 sqpERKNTGFMLMCEVALGEMNAITQAEYMEK-APQGFHSTKGIGQRGPDPSKTIVVPSGVTIPVGEImqYPKTPGHHYG 2546
Cdd:cd01437 250 ---ASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKP--VPSGHKTDTS 324
|
....
gi 470409102 2547 LQHN 2550
Cdd:cd01437 325 LLYN 328
|
|
| PLN03124 |
PLN03124 |
poly [ADP-ribose] polymerase; Provisional |
1957-2551 |
4.03e-86 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 297.13 E-value: 4.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1957 DWEHDSAELLNNPPEPSDEEKAEQQEKAREKQ------KHAHPVDKNFDQRQNSEVYAENKG-EVYDVTLTTVDVRYGTh 2029
Cdd:PLN03124 112 ALESDVKVGSANGTGEDEKEKGGDEEREKEEKivtatkKGRAVLDQWLPDHIKSNYHVLEEGdDVYDAMLNQTNVGDNN- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2030 giNNFYKMQVIHNKLKDFYILWTRWGRIGDVGQYQ-RTPFPTAEATVEEFKKIFKAKTGNSWEDRANFEKKPKKYHMIKL 2108
Cdd:PLN03124 191 --NKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKlHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEM 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2109 ETNKEKLVANLLKPFDIELEDEaqgggaaadahakplsvasrypPSKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMP 2188
Cdd:PLN03124 269 DYEDEEESKKDKPSVSSEDKNK----------------------QSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2189 LGRLTRDGIDAAMQIiadLRKlirevpICAALrgrhsyhdDKEGEeeenaveeanaeadngangegtkkkkkkkeltlee 2268
Cdd:PLN03124 327 LGKLSKSTILKGYEV---LKR------IAEVI--------SRSDR----------------------------------- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2269 mrelyEEIAELSNRFYELIPH-------AEYTIesipplNTNDLLNKKAQpshdhtLLSNLAEIRTAAKILLGAHYrvKE 2341
Cdd:PLN03124 355 -----ETLEELSGEFYTVIPHdfgfkkmRQFTI------DTPQKLKHKLE------MVEALGEIEIATKLLKDDIG--EQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2342 INPLDYCYSAMHIRLSQLPKETDEYKILRQYIKR------SSPSVFVTNIYHLQRKGEPERFQeRWEKVPNHQLLFHGSA 2415
Cdd:PLN03124 416 DDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENthgqthSGYTLEIVQIFKVSREGEDERFQ-KFSSTKNRMLLWHGSR 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2416 LSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCrmgHTGSrhsqpeRKNTGFMLMCEVALGEMNAITQAE 2495
Cdd:PLN03124 495 LTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYC---YASA------ANPDGVLLLCEVALGDMNELLQAD 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 2496 Y-MEKAPQGFHSTKGIGQRGPDPSKTIVVPSGVTIPVGEIMQYPKTPGhhyGLQHND 2551
Cdd:PLN03124 566 YnANKLPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGKPVESPYSKG---SLEYNE 619
|
|
| PLN03123 |
PLN03123 |
poly [ADP-ribose] polymerase; Provisional |
2009-2532 |
9.24e-71 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215590 [Multi-domain] Cd Length: 981 Bit Score: 259.34 E-value: 9.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2009 ENKGEVYDVTLTTVDVrygTHGINNFYKMQVIH-NKLKDFYIlWTRWGRIGD--VGQYQRTPFPTAEAtVEEFKKIFKAK 2085
Cdd:PLN03123 514 EDGKSIYNTTLNMSDL---STGVNSYYILQIIEeDKGSDCYV-FRKWGRVGNekIGGNKLEEMSKSDA-IHEFKRLFLEK 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2086 TGN---SWEDRANFEKKPKKYHmikletnkeklvanllkPFDIELedeaqgGGAAADAHAKPLSVASRYPPSKLPLsiqh 2162
Cdd:PLN03123 589 TGNpweSWEQKTNFQKQPGKFY-----------------PLDIDY------GVNEQPKKKAASGSKSNLAPRLVEL---- 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2163 aIKALTDSSMLTQAMQTEGIDTEAMPLGRLTRDGIDAAMQIIADLRKLIREvpicaalrgrhSYHDdkegeeeenaveea 2242
Cdd:PLN03123 642 -MKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKE-----------NDQD-------------- 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2243 naeadngangegtkkkkkkkeltlEEMRElyEEIAELSNRFYELIPhaeytieSIPP--LNTNDLLNKKAQpshdhtLLS 2320
Cdd:PLN03123 696 ------------------------PSIRE--SLLVDASNRFFTLIP-------SIHPhiIRDEDDLKSKVK------MLE 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2321 NLAEIRTAAKiLLGahYRVKEINPLDYCYSAMHIRLSQLPKETDEYKILRQYIKRS-SP-----SVFVTNIYHLQRKGEP 2394
Cdd:PLN03123 737 ALQDIEIASR-LVG--FDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTThAPthtdwSLELEEVFSLEREGEF 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2395 ERFQERWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCRMghtgsrhsqpERKN 2474
Cdd:PLN03123 814 DKYAPYKEKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYT----------DRKN 883
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 470409102 2475 -TGFMLMCEVALGEMNAITQAEYMEKAPQGFHSTKGIGQRGPDPSKTIVVPSGVTIPVG 2532
Cdd:PLN03123 884 pVGLMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCG 942
|
|
| PARP |
pfam00644 |
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
2363-2533 |
2.38e-57 |
|
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.
Pssm-ID: 395519 [Multi-domain] Cd Length: 195 Bit Score: 197.56 E-value: 2.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2363 TDEYKILRQYIKRSSPSV-----FVTNIYHLQRKGEPERFQErWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFS 2437
Cdd:pfam00644 1 SEEYQIIEKYFLSTHDPThgyplFILEIFRVQRDGEWERFQP-KKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2438 GYAFGKGIYFADMFQKSFGYCRMGHTgsrhsqperKNTGFMLMCEVALGEMNAITQAEYMEKAPQGFHSTKGIGQRGPDP 2517
Cdd:pfam00644 80 GYMFGKGIYFADDASKSANYCPPSEA---------HGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES 150
|
170
....*....|....*..
gi 470409102 2518 SKTIV-VPSGVTIPVGE 2533
Cdd:pfam00644 151 FVDLDgVPLGKLVATGY 167
|
|
| WGR_PARP |
cd07997 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
2011-2110 |
3.69e-42 |
|
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.
Pssm-ID: 153426 Cd Length: 102 Bit Score: 150.15 E-value: 3.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2011 KGEVYDVTLTTVDVRYGthgINNFYKMQVIHNKLKDFYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSW 2090
Cdd:cd07997 6 IATVYDATLNQTDISNN---NNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEW 82
|
90 100
....*....|....*....|
gi 470409102 2091 EDRANFEKKPKKYHMIKLET 2110
Cdd:cd07997 83 ENRPLFKKQPGKYALVELDY 102
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1228-1508 |
3.39e-40 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 151.65 E-value: 3.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1228 TALHFLVSQPDLLSDFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAM 1307
Cdd:COG0666 23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1308 VDALLQANTDVD-KWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNAS 1386
Cdd:COG0666 103 VKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1387 DNNGSSGLHYAVTYaepgadASFEIEDFLLKKGANVNKRDNHGRVPLHYAfLKTGNQNtpidpietVSSLCAVRDLEIDV 1466
Cdd:COG0666 183 DNDGETPLHLAAEN------GHLEIVKLLLEAGADVNAKDNDGKTALDLA-AENGNLE--------IVKLLLEAGADLNA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 470409102 1467 ADNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPL 1508
Cdd:COG0666 248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1239-1530 |
5.91e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1239 LLSDFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDV 1318
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1319 D-KWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYA 1397
Cdd:COG0666 81 NaKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1398 VTYAEPgadasfEIEDFLLKKGANVNKRDNHGRVPLHYAFLKtGNqntpidpIETVSSLCAvRDLEIDVADNHKRTPLHY 1477
Cdd:COG0666 161 AANGNL------EIVKLLLEAGADVNARDNDGETPLHLAAEN-GH-------LEIVKLLLE-AGADVNAKDNDGKTALDL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1478 AAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANV 1530
Cdd:COG0666 226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
751-982 |
6.85e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 6.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVA 830
Cdd:COG0666 56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 831 LNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLEQPsVDVNI 910
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG-ADVNA 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 911 RDDDGRTLAsqlmDIVCESSHKQLQYLIEKKSADVTTPDTKGLTPLHYVAQNFDPVQAAAEFKADNDNSDAD 982
Cdd:COG0666 215 KDNDGKTAL----DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
741-982 |
9.79e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 124.30 E-value: 9.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 741 IDTKSKGSRFTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVI 820
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 821 HAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFL 900
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 901 LEQPsVDVNIRDDDGRTLasqLMDIVCESSHKQLQYLIEKKsADVTTPDTKGLTPLHYVAQNFDPVQAAAEFKADNDNSD 980
Cdd:COG0666 173 LEAG-ADVNARDNDGETP---LHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
|
..
gi 470409102 981 AD 982
Cdd:COG0666 248 KD 249
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
765-1122 |
3.75e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 765 VKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVALNYLLRMSAAACCA 844
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 845 DSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLEQPsVDVNIRDDDGRTLasqLMD 924
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTP---LHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 925 IVCESSHKQLQYLIEKKsADVTTPDTKGLTPLHYVAQNfdpvqaaaefkadndnsdadstspsvnagkddmdvdgkdkgk 1004
Cdd:COG0666 160 AAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAEN------------------------------------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1005 ekGDDDkeevgendepkkkkkktwtnwsvvIAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQIAAIHV 1084
Cdd:COG0666 197 --GHLE------------------------IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
330 340 350
....*....|....*....|....*....|....*...
gi 470409102 1085 QDRNVLHQLTPQLMERDLLPLLEAIARNVGEQRFKEMA 1122
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1223-1427 |
3.75e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1223 TDGRRTALHFLVSQPDL-LSDFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVN 1301
Cdd:COG0666 84 DDGGNTLLHAAARNGDLeIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1302 RQNLAMVDALLQANTDVD-KWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAG 1380
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 470409102 1381 ADVNASDNNGSSGLHYAVTYAEPGADASFEIEDFLLKKGANVNKRDN 1427
Cdd:COG0666 243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1250-1569 |
1.01e-28 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 122.83 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1250 DINAQDRKMETPLHLAIN---GDRQDVFNMLLaESSINANVADSLGTLPLHLAV-NRQNLAMVDALLQANTDVDKWQR-G 1324
Cdd:PHA03095 39 DVNFRGEYGKTPLHLYLHyssEKVKDIVRLLL-EAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIKAGADVNAKDKvG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1325 RAALHT--AVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKN--MNLVRILVQAGADVNASDNNGSSGLHYAVTY 1400
Cdd:PHA03095 118 RTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1401 AEPGADASFEiedfLLKKGANVNKRDNHGRVPLHYAFLKTGNQNTPIDP--IETVSslcavrdleIDVADNHKRTPLHYA 1478
Cdd:PHA03095 198 FKPRARIVRE----LIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGIS---------INARNRYGQTPLHYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1479 AQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANVrHPIYNVtwgFAHDENQRHKRVIThsTS 1558
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA-ETVAAT---LNTASVAGGDIPSD--AT 338
|
330
....*....|.
gi 470409102 1559 RSMFYEAVSRG 1569
Cdd:PHA03095 339 RLCVAKVVLRG 349
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
660-885 |
9.32e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.82 E-value: 9.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 660 LKLLLDRGVSHREVDREGSTSLMIAAQCGRLDSIKLLLdwdsrkmaeaekeaeesdkEHSSDddeeeeaprkqpraklvp 739
Cdd:COG0666 103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------------EAGAD------------------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 740 yIDTKSKgSRFTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAV 819
Cdd:COG0666 146 -VNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 820 IHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPL 885
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| WGR |
smart00773 |
Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
2011-2097 |
5.65e-25 |
|
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.
Pssm-ID: 214814 Cd Length: 84 Bit Score: 100.44 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2011 KGEVYDVTLTTVDvryGTHGINNFYKMQVIHNKLKDfYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSW 2090
Cdd:smart00773 2 GGEIYDVYLNFTD---LASNNNKFYIIQLLEDDFGG-YSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGY 77
|
....*..
gi 470409102 2091 EDRANFE 2097
Cdd:smart00773 78 EERGKFV 84
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1337-1762 |
2.29e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 109.34 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1337 LAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNL---VRILVQAGADVNASDNNGSSGLHYAVTYAEpgadaSFEIED 1413
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAT-----TLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1414 FLLKKGANVNKRDNHGRVPLHyAFLKTGNQNTPIdpIEtvsslcavrdleidvadnhkrtplhyaaqrgattcslLLLNR 1493
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLH-VYLSGFNINPKV--IR-------------------------------------LLLRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1494 KAGLENQDEDGNTPLGLGLKNGHGDYAIV--LLQKNANVrhpiynvtwgFAHDENqrhKRVITHSTSRSmfyeavSRGWQ 1571
Cdd:PHA03095 142 GADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADV----------YAVDDR---FRSLLHHHLQS------FKPRA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1572 GVSYMMLDAGLDkltaltdaintgkfqlvvtllsktpedevVQGLDADDRTLFHHLANYCSGKldhwaQTLAEKLEERGV 1651
Cdd:PHA03095 203 RIVRELIRAGCD-----------------------------PAATDMLGNTPLHSMATGSSCK-----RSLVLPLLIAGI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1652 AMNVIDKHGRLPLHYASKNGCGVLVDFFLKRSkSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKN 1731
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTAS 327
|
410 420 430
....*....|....*....|....*....|....*
gi 470409102 1732 QAHGRHNTPEKKQRRHA----KAAAALSKVAQETH 1762
Cdd:PHA03095 328 VAGGDIPSDATRLCVAKvvlrGAFSLLPEPIRAYH 362
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
795-1125 |
3.99e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 105.04 E-value: 3.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 795 VDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADP 874
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 875 NAPNDWKTTPLAIALQKGHLACADFLLEQPsVDVNIRDDDGRTLasqLMDIVCESSHKQLQYLIEKKsADVTTPDTKGLT 954
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETP---LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 955 PLHYVAQNfdpvqaaaefkadndnsdadstspsvnagkddmdvdgkdkgkekGDDDkeevgendepkkkkkktwtnwsvv 1034
Cdd:COG0666 156 PLHLAAAN--------------------------------------------GNLE------------------------ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQIAAIHVQDRNVLHQLTPQLMERDLLPLLEAIARNVG 1114
Cdd:COG0666 168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
|
330
....*....|.
gi 470409102 1115 EQRFKEMAREL 1125
Cdd:COG0666 248 KDKDGLTALLL 258
|
|
| WGR_PARP2_like |
cd08003 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
2006-2108 |
4.22e-24 |
|
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis.
Pssm-ID: 153430 Cd Length: 103 Bit Score: 98.94 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2006 VYAENKgEVYDVTLTTVDVRYGThgiNNFYKMQVIHNKLKDFYILWTRWGRIGDVGQYQRTPFPT-AEATVEEFKKIFKA 2084
Cdd:cd08003 2 VYEEGD-DVYDAMLNQTNIQQNN---NKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSdLEQAKSLFEKKFLD 77
|
90 100
....*....|....*....|....
gi 470409102 2085 KTGNSWEDRANFEKKPKKYHMIKL 2108
Cdd:cd08003 78 KTKNEWEDRANFEKVAGKYDLLEM 101
|
|
| WGR_PARP3_like |
cd08002 |
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ... |
2003-2110 |
9.20e-24 |
|
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage.
Pssm-ID: 153429 Cd Length: 100 Bit Score: 97.86 E-value: 9.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2003 NSEVYaenkgEVYDVTLTTVDVRygtHGINNFYKMQVIHNKlkDFYILWTRWGRIGDVGQYQ-RTPFPTAEATVEEFKKI 2081
Cdd:cd08002 2 GAEVD-----EDYDCMLNQTNIG---HNNNKFYVIQLLESG--KEYYVWNRWGRVGEKGQNKlKGPWDSLEGAIKDFEKK 71
|
90 100
....*....|....*....|....*....
gi 470409102 2082 FKAKTGNSWEDRANFEKKPKKYHMIKLET 2110
Cdd:cd08002 72 FKDKTKNNWEDRENFVPHPGKYTLIEMDY 100
|
|
| WGR |
pfam05406 |
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
2015-2097 |
1.15e-23 |
|
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.
Pssm-ID: 398851 Cd Length: 79 Bit Score: 96.54 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2015 YDVTLTTVDVRYGThgiNNFYKMQvIHNKLKDFYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKTGNSWEDRA 2094
Cdd:pfam05406 1 YDLYLEQTDAARNS---NKFYEIQ-VEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERG 76
|
...
gi 470409102 2095 NFE 2097
Cdd:pfam05406 77 EFE 79
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1642-1935 |
8.69e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.10 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1642 LAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADcs 1721
Cdd:COG0666 69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1722 aldarvkqknqahgrhntpekkqrrhakaaaalskvaqethlviyamrasladllnlllankadLNAKDSLGNTCLIYAV 1801
Cdd:COG0666 146 ----------------------------------------------------------------VNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1802 RNNDTDMVHLLftkrrgaakpgpssssssssappsslspaepelmLENetGIDPNVQDEQGKTALHHVVSpldYGSYENV 1881
Cdd:COG0666 162 ANGNLEIVKLL----------------------------------LEA--GADVNARDNDGETPLHLAAE---NGHLEIV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1882 ALLtmlLKAGADPNVKDNQGHTPLYYALQQRDGVMAARLRSLGAKLDKKEEANL 1935
Cdd:COG0666 203 KLL---LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
|
|
| PLN03122 |
PLN03122 |
Poly [ADP-ribose] polymerase; Provisional |
1915-2535 |
1.31e-21 |
|
Poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 102.95 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1915 VMAARLRSLG--AKLDKKEEANLPrqasfVLSDQWISD--YGIPPVDWE-HDSAELLNNPPEPSDEEKAEQQEKARE--- 1986
Cdd:PLN03122 230 VVSPAERERGgsSKIAEAMERGIP-----VVREAWLIDsiEKQEAQPLEaYDVVSDLSVEGRGIPWDKQDPSEEAIEsls 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1987 ---KQKHAHPVDKNFD-QRQNSEVYaENKGEVYDVTLTTVDVrygTHGINNFYKMQVIHNKLKDFYILWTRwGRIGD-VG 2061
Cdd:PLN03122 305 aelKLYGKRGVYKDSKlQEEGGKIF-EKDGILYNCAFSICDL---GRGLNEYCIMQLITVPDSNLHLYYKK-GRVGDdPN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2062 QYQRT-PFPTAEATVEEFKKIFKAKTGN---SWEDRANFEKKPKKYHMIKLETNKEKLVANLlkpfdieledeaqgggaa 2137
Cdd:PLN03122 380 AEERLeEWEDVDAAIKEFVRLFEEITGNefePWEREKKFEKKRLKFYPIDMDDGVDVRAGGL------------------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2138 adaHAKPLSVASRYppSKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMPLGRLT----RDGIDAAMQIIADLRKLIRE 2213
Cdd:PLN03122 442 ---GLRQLGVAAAH--CKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSdfhlKRCEEVLLEFAEFVKSEKET 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2214 VPICAALrgrhsyhddkegeeeenaveeanaeadngangegtkkkkkkkeltleemrelyeeIAELSNRFYELIPhaeyt 2293
Cdd:PLN03122 517 GQKAEAM-------------------------------------------------------WLDFSNKWFSLVH----- 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2294 ieSIPPLNTNDLlNKKAQpsHDHTLLSNLAEIRTAAKiLLGAHYRVKEINPLDYCYSAMHIRLSQLPKETDEYKILRQYI 2373
Cdd:PLN03122 537 --STRPFVIRDI-DELAD--HAASALETVRDINVASR-LIGDMTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYL 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2374 KR---------SSPSVFVTNIYHLQRKGEPErfQERWEKVPNHQLLFHGSALSNFVGILSQGLRIAPPEAPFSGYAFGKG 2444
Cdd:PLN03122 611 EKtyepvkvgdVSYSVSVENIFAVESSAGPS--LDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKA 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2445 IYFADMFQKSFGYcrmGHTGSrhSQPErkntGFMLMCEVALG-EMNAITQAE----YMEKAPQGfhsTKGIGQRGPDPSK 2519
Cdd:PLN03122 689 IVCSDAAAEAARY---GFTAV--DRPE----GFLVLAVASLGdEVLELTKPPedvkSYEEKKVG---VKGLGRKKTDESE 756
|
650
....*....|....*.
gi 470409102 2520 TIVVPSGVTIPVGEIM 2535
Cdd:PLN03122 757 HFKWRDDITVPCGRLI 772
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1250-1528 |
1.82e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 100.04 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1250 DINAQDRKMETPLHLAINGDRQDVFNMLLaESSINANVadslgtlplhLAVNRQNLAMVDALLQANTDVD-KWQRGRAAL 1328
Cdd:PHA02874 60 DINHINTKIPHPLLTAIKIGAHDIIKLLI-DNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNiKDAELKTFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1329 HTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEpgadas 1408
Cdd:PHA02874 129 HYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1409 FEIEDFLLKKGANVNKRDNHGRVPLHYAFLktgnQNTPIDPIetvsslcAVRDLEIDVADNHKRTPLHYAAQrgaTTCSL 1488
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTPLHNAII----HNRSAIEL-------LINNASINDQDIDGSTPLHHAIN---PPCDI 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 470409102 1489 ----LLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNA 1528
Cdd:PHA02874 269 diidILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANA 312
|
|
| PARP_reg |
pfam02877 |
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ... |
2154-2349 |
1.95e-21 |
|
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.
Pssm-ID: 460732 [Multi-domain] Cd Length: 135 Bit Score: 92.20 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2154 SKLPLSIQHAIKALTDSSMLTQAMQTEGIDTEAMPLGRLTRDGIDAAMQIIADLRKLIREVPICAALrgrhsyhddkege 2233
Cdd:pfam02877 1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAKAK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2234 eeenaveeanaeadngangegtkkkkkkkeltleemrelyEEIAELSNRFYELIPHAeYTIESIPPLNTNDLLNKKAQps 2313
Cdd:pfam02877 68 ----------------------------------------AKLEDLSNRFYTLIPHD-FGRNRPPVIDTEEELKEKLE-- 104
|
170 180 190
....*....|....*....|....*....|....*.
gi 470409102 2314 hdhtLLSNLAEIRTAAKILLGAHYrVKEINPLDYCY 2349
Cdd:pfam02877 105 ----LLEALLDIEVASKLLKDSKS-DDDEHPLDRHY 135
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1244-1439 |
9.53e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 97.81 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1244 IHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVN-----RQNLAMVDALLQANTDV 1318
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1319 DK-WQRGRAALHTAVDCC--NLAIINSLLRAKANVNIQDSQHKTPLHYALQ--RKNMNLVRILVQAGADVNA-------- 1385
Cdd:PHA03100 100 NApDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAknrvnyll 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1386 --------SDNNGSSGLHYAVTYAEPgadasfEIEDFLLKKGANVNKRDNHGRVPLHYAFLK 1439
Cdd:PHA03100 180 sygvpiniKDVYGFTPLHYAVYNNNP------EFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1328-1532 |
4.54e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 95.50 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1328 LHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRK-----NMNLVRILVQAGADVNASDNNGSSGLHYAVTYAE 1402
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1403 pgadASFEIEDFLLKKGANVNKRDNHGRVPLHYaFLKTGNQNTPIdpIET-------VSSLCAVR-----DLEIDVADNH 1470
Cdd:PHA03100 119 ----NSYSIVEYLLDNGANVNIKNSDGENLLHL-YLESNKIDLKI--LKLlidkgvdINAKNRVNyllsyGVPINIKDVY 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1471 KRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANVRH 1532
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| WGR_PARP1_like |
cd08001 |
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ... |
2006-2106 |
1.45e-19 |
|
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging.
Pssm-ID: 153428 [Multi-domain] Cd Length: 104 Bit Score: 85.72 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2006 VYAENKGEVYDVTLTTVDVrygTHGINNFYKMQVI-HNKLKDFYiLWTRWGRIG-DVGQYQRTPFPTAEATVEEFKKIFK 2083
Cdd:cd08001 2 HVLEEGGNLYSAVLGLVDI---QTGTNSYYKLQLLeHDKGNRYW-VFRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYE 77
|
90 100
....*....|....*....|...
gi 470409102 2084 AKTGNSWEDRANFEKKPKKYHMI 2106
Cdd:cd08001 78 EKTGNDFENRKNFKKKPGKFYPL 100
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1678-1930 |
3.65e-19 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.40 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1678 FFLKRSKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKNQAHGRHNTPEKKQRRHAKAAAALSKV 1757
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1758 AQETHLVIYAMRASLADLLNLLLANKADLNAKDSLGNTCLIYAVRNNDTDMVHLLftkrrgaakpgpssssssssappss 1837
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1838 lspaepelmLENetGIDPNVQDEQGKTALHHVVSpldygsYENVALLTMLLKAGADPNVKDNQGHTPLYYALQQRDGVMA 1917
Cdd:COG0666 140 ---------LEA--GADVNAQDNDGNTPLHLAAA------NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250
....*....|...
gi 470409102 1918 ARLRSLGAKLDKK 1930
Cdd:COG0666 203 KLLLEAGADVNAK 215
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1237-1437 |
3.01e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 90.02 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1237 PDLLSDFIH---EYKLDINAQDRKMETPLHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQ 1313
Cdd:PHA02874 100 PCIEKDMIKtilDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1314 --ANTDVDKWQrGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRkNMNLVRILVQaGADVNASDNNGS 1391
Cdd:PHA02874 179 kgAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQDIDGS 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 470409102 1392 SGLHYAVTYAepgadASFEIEDFLLKKGANVNKRDNHGRVPLHYAF 1437
Cdd:PHA02874 256 TPLHHAINPP-----CDIDIIDILLYHKADISIKDNKGENPIDTAF 296
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1221-1436 |
3.70e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.28 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1221 SLTDGRRTALHFLVSQPDL--LSDFIHEYKLDINAQDRKMETPLHL-AING-DRQDVFNMLLAESSINAnvADSLGTLPL 1296
Cdd:PHA02876 268 SIDDCKNTPLHHASQAPSLsrLVPKLLERGADVNAKNIKGETPLYLmAKNGyDTENIRTLIMLGADVNA--ADRLYITPL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1297 HlavnrqnlamvdallQANTdVDKWQRgraalhtavdccnlaIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRIL 1376
Cdd:PHA02876 346 H---------------QAST-LDRNKD---------------IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1377 VQAGADVNASDNNGSSGLHYAVTYAEPgadasFEIEDFLLKKGANVNKRDNHGRVPLHYA 1436
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFALCGTNP-----YMSVKTLIDRGANVNSKNKDLSTPLHYA 449
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1211-1428 |
1.11e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 88.18 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1211 PQPKQSPGKYSLTDGRRTAlhflvsqpdllsDFIHEYKLDINAQDRKMETPLHLAINGDRQDvFNM--LLAESSINANVA 1288
Cdd:PHA03100 71 PLHYLSNIKYNLTDVKEIV------------KLLLEYGANVNAPDNNGITPLLYAISKKSNS-YSIveYLLDNGANVNIK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1289 DSLGTLPLHLAV--NRQNLAMVDALLQANTDVDKWQRgraalhtavdccnlaiINSLLRAKANVNIQDSQHKTPLHYALQ 1366
Cdd:PHA03100 138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR----------------VNYLLSYGVPINIKDVYGFTPLHYAVY 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1367 RKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEPgadasfEIEDFLLKKGANVNKRDNH 1428
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK------EIFKLLLNNGPSIKTIIET 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1228-1437 |
1.77e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.16 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1228 TALHFLV---SQPDLLsDFIHEYKLDINAQDRKMETPLHLAINGD--RQDVFNMLLAESsINANVADSLGTLPLHLAV-- 1300
Cdd:PHA03095 85 TPLHLYLynaTTLDVI-KLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKG-ADVNALDLYGMTPLAVLLks 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1301 NRQNLAMVDALLQANTDV-DKWQRGRAALHTAVDCC--NLAIINSLLRAKANVNIQDSQHKTPLHYALQ--RKNMNLVRI 1375
Cdd:PHA03095 163 RNANVELLRLLIDAGADVyAVDDRFRSLLHHHLQSFkpRARIVRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLP 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1376 LVQAGADVNASDNNGSSGLHYAVTYAEPGAdasFeieDFLLKKGANVNKRDNHGRVPLHYAF 1437
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRA---C---RRLIALGADINAVSSDGNTPLSLMV 298
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1033-1400 |
4.85e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.81 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1033 VVIAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQIAAIHVQDRNVLHqltpQLMERDLLPLLEAIARN 1112
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE----CAVDSKNIDTIKAIIDN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1113 VGEQRFKEMA-----RELDDEgfTPFLRFVQHYGIWSPDHKAKVP-SRTKQAPPVvnpeerrrqekaardrfRRFLVRFI 1186
Cdd:PHA02876 234 RSNINKNDLSllkaiRNEDLE--TSLLLYDAGFSVNSIDDCKNTPlHHASQAPSL-----------------SRLVPKLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1187 ELGAvDTTApvrstkawRDWKKADPQPKQSPGKYSlTDGRRTalhfLVSQpdllsdfiheyKLDINAQDRKMETPLHLAI 1266
Cdd:PHA02876 295 ERGA-DVNA--------KNIKGETPLYLMAKNGYD-TENIRT----LIML-----------GADVNAADRLYITPLHQAS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1267 NGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKW-QRGRAALHTAVDCCN-LAIINSLL 1344
Cdd:PHA02876 350 TLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALsQKIGTALHFALCGTNpYMSVKTLI 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 1345 RAKANVNIQDSQHKTPLHYALQRK-NMNLVRILVQAGADVNASDNNGSSGLHYAVTY 1400
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY 486
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1337-1706 |
8.39e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.04 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1337 LAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTyaepgaDASFEIEDFLL 1416
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD------SKNIDTIKAII 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1417 KKGANVNKRDnhgrvplhYAFLKtGNQNTPIDpietVSSLCAVRDLEIDVADNHKRTPLHYAAQrgATTCSLL---LLNR 1493
Cdd:PHA02876 232 DNRSNINKND--------LSLLK-AIRNEDLE----TSLLLYDAGFSVNSIDDCKNTPLHHASQ--APSLSRLvpkLLER 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1494 KAGLENQDEDGNTPLGLGLKNGHGDYAI---VLLQKNANVRHPIYNVTWGFAHDENQRHKRVIT------------HSTS 1558
Cdd:PHA02876 297 GADVNAKNIKGETPLYLMAKNGYDTENIrtlIMLGADVNAADRLYITPLHQASTLDRNKDIVITllelganvnardYCDK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1559 RSMFYEAVsRGWQGVSYMMLDAGLDkLTALTDAINTGkfqLVVTLLSKTPedevvqgldaddrtlfhhlanYCSGKldhw 1638
Cdd:PHA02876 377 TPIHYAAV-RNNVVIINTLLDYGAD-IEALSQKIGTA---LHFALCGTNP---------------------YMSVK---- 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 1639 aqtlaeKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRSKSDVNLIDENGKSPLVYAvLGSH 1706
Cdd:PHA02876 427 ------TLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYH 487
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
753-878 |
4.51e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.54 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 753 LHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEagcnieaadklkrtaviHAARNgqlvaln 832
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-----------------HADVN------- 56
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 470409102 833 yllrmsaaaccADSSTNTAAHYAAAFGWRACLELLVENGADPNAPN 878
Cdd:pfam12796 57 -----------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1239-1562 |
8.39e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 83.96 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1239 LLSDFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSiNANVADSLGTLPLHLAVNRQNLAMVDALLQANTDV 1318
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1319 DK--------------------WQRG----------RAALHTAVDCCNLA-IINSLLRAKANVNIQDSQHKTPLHyaLQR 1367
Cdd:PHA02876 238 NKndlsllkairnedletslllYDAGfsvnsiddckNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLY--LMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1368 KN---MNLVRILVQAGADVNASDNNGSSGLHYAVTYaepgaDASFEIEDFLLKKGANVNKRDNHGRVPLHYAFLKtgnQN 1444
Cdd:PHA02876 316 KNgydTENIRTLIMLGADVNAADRLYITPLHQASTL-----DRNKDIVITLLELGANVNARDYCDKTPIHYAAVR---NN 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1445 TPIdpIETVSSLCAvrdlEIDVADNHKRTPLHYAAQRGATTCSL-LLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVL 1523
Cdd:PHA02876 388 VVI--INTLLDYGA----DIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEM 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 1524 LQKNA------NVR-----------HPIYNVTWGFAHDenQRHKRVITHSTSRSMF 1562
Cdd:PHA02876 462 LLDNGadvnaiNIQnqypllialeyHGIVNILLHYGAE--LRDSRVLHKSLNDNMF 515
|
|
| ADP_ribosyl |
cd01341 |
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ... |
2410-2488 |
3.54e-15 |
|
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.
Pssm-ID: 238651 [Multi-domain] Cd Length: 137 Bit Score: 74.52 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2410 LFHGSALSNFVGILSQGLRIAPPEAPFSGYAFGKGIYFADMFQKSFGYCRMGHTGSRHSQPERK-------NTGFMLMCE 2482
Cdd:cd01341 2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKvcgrelcVFGFLTLGV 81
|
....*.
gi 470409102 2483 VALGEM 2488
Cdd:cd01341 82 MSGATE 87
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
740-922 |
3.58e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.84 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 740 YIDTKSKgSRFTALHFAVRNNQPEAV-KLLIEKGAHIEAPDVNRMTPLhHAVALGF---VDVAKELVEAGCNIEAADKLK 815
Cdd:PHA03095 75 DVNAPER-CGFTPLHLYLYNATTLDViKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 816 RTAV-----------------------IHAARNGQLVALNYLL----------RMSAAACC----ADSSTNTAAHYAAAF 858
Cdd:PHA03095 153 MTPLavllksrnanvellrllidagadVYAVDDRFRSLLHHHLqsfkprarivRELIRAGCdpaaTDMLGNTPLHSMATG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470409102 859 GW--RACLELLVENGADPNAPNDWKTTPL---AIALQKGhlACaDFLLEQPSvDVNIRDDDGRTLASQL 922
Cdd:PHA03095 233 SSckRSLVLPLLIAGISINARNRYGQTPLhyaAVFNNPR--AC-RRLIALGA-DINAVSSDGNTPLSLM 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
751-1082 |
3.58e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.84 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQP---EAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFV-DVAKELVEAGCNIEAADKLKRTAvIHaarng 826
Cdd:PHA03095 49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTP-LH----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 827 qlvalnyllrmsaaACCADSSTNTAAhyaaafgwracLELLVENGADPNAPNDWKTTPLAIalqkghlacadfLLEQPSV 906
Cdd:PHA03095 123 --------------VYLSGFNINPKV-----------IRLLLRKGADVNALDLYGMTPLAV------------LLKSRNA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 907 DVNIrdddgrtlasqlmdivcesshkqLQYLIeKKSADVTTPDTKGLTPLHYVAQNFDPvqaaaefkadndnsDADSTSP 986
Cdd:PHA03095 166 NVEL-----------------------LRLLI-DAGADVYAVDDRFRSLLHHHLQSFKP--------------RARIVRE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 987 SVNAGKDDMDVDgkdkgkekgdddkeeVGENDEPKKKKKKTWTNWSVVIAkmLIKHGADVNAQTKDKSTPLMLAKTRDNE 1066
Cdd:PHA03095 208 LIRAGCDPAATD---------------MLGNTPLHSMATGSSCKRSLVLP--LLIAGISINARNRYGQTPLHYAAVFNNP 270
|
330
....*....|....*.
gi 470409102 1067 ELLILLLDNGAQIAAI 1082
Cdd:PHA03095 271 RACRRLIALGADINAV 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1583-1795 |
7.74e-15 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 77.69 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1583 DKLTALTDAINTGKFQLVVTLLSKTPEDEVVqglDADDRTLFHHLANYcsGKLDhwaqtLAEKLEERGVAMNVIDKHGRL 1662
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLEAGADVNAR---DKDGETPLHLAAYN--GNLE-----IVKLLLEAGADVNAQDNDGNT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1663 PLHYASKNGCGVLVDFFLKRsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKNQAHGRHNTPEK 1742
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1743 KQRRHAKAAAALSKVAQETHLVIYAMRASLADLLNLLLANKADLNAKDSLGNT 1795
Cdd:COG0666 235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1328-1426 |
9.85e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1328 LHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQaGADVNaSDNNGSSGLHYAVTYaepgadA 1407
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARS------G 72
|
90
....*....|....*....
gi 470409102 1408 SFEIEDFLLKKGANVNKRD 1426
Cdd:pfam12796 73 HLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1250-1423 |
1.60e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.41 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1250 DINAQDrkMETPLHLAI-NGDRQDVFNMLLAESSINaNVADSLGTLPLHLAVNRQNLAMVDALLQ--ANTDVDKWQRgRA 1326
Cdd:PHA02875 62 DVKYPD--IESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIArgADPDIPNTDK-FS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1327 ALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGS-SGLHYAVTYAEPga 1405
Cdd:PHA02875 138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKI-- 215
|
170
....*....|....*...
gi 470409102 1406 dasfEIEDFLLKKGANVN 1423
Cdd:PHA02875 216 ----DIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
820-912 |
3.08e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.45 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 820 IHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENgADPNAPNDwKTTPLAIALQKGHLACADF 899
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79
|
90
....*....|...
gi 470409102 900 LLEQpSVDVNIRD 912
Cdd:pfam12796 80 LLEK-GADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
681-812 |
5.16e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 66.68 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 681 LMIAAQCGRLDSIKLLLDwdsrkmaeaekeaEESDKEHSSDDDEeeeaprkqpraklvpyidtkskgsrfTALHFAVRNN 760
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE-------------NGADANLQDKNGR--------------------------TALHLAAKNG 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 470409102 761 QPEAVKLLIEKgAHIEAPDvNRMTPLHHAVALGFVDVAKELVEAGCNIEAAD 812
Cdd:pfam12796 42 HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1275-1763 |
8.92e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.52 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1275 NMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQD 1354
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1355 SQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEPgadasfEIEDFLLKKGANVNKRDNHGRvplh 1434
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL------EIVKLLLEAGADVNAQDNDGN---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1435 yaflktgnqntpidpietvsslcavrdleidvadnhkrTPLHYAAQrgattcsllllnrkaglenqdedgntplglglkN 1514
Cdd:COG0666 155 --------------------------------------TPLHLAAA---------------------------------N 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1515 GHGDYAIVLLQKNANVrhpiynvtwgfahdenqrhkrvithstsrsmfyeavsrgwqgvsymmldagldkltaltdaint 1594
Cdd:COG0666 164 GNLEIVKLLLEAGADV---------------------------------------------------------------- 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1595 gkfqlvvtllsktpedevvqgldaddrtlfhhlanycsgkldhwaqtlaekleergvamNVIDKHGRLPLHYASKNGCGV 1674
Cdd:COG0666 180 -----------------------------------------------------------NARDNDGETPLHLAAENGHLE 200
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1675 LVDFFLKRsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKNQAHGRHNTPEKKQRRHAKAAAAL 1754
Cdd:COG0666 201 IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
....*....
gi 470409102 1755 SKVAQETHL 1763
Cdd:COG0666 280 AALLDLLTL 288
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
660-779 |
1.09e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 660 LKLLLDRGVSHREVDREGSTSLMIAAQCGRLDSIKLLLDwdsrkmaeaekeaeesdkehssdddeeeeaprkqpraklvp 739
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------------------- 51
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 470409102 740 YIDTKSKGSRFTALHFAVRNNQPEAVKLLIEKGAHIEAPD 779
Cdd:pfam12796 52 HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1262-1354 |
1.24e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.52 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1262 LHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQaNTDVDKWQRGRAALHTAVDCCNLAIIN 1341
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 470409102 1342 SLLRAKANVNIQD 1354
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1261-1513 |
1.71e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1261 PLHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKWQRGRA---ALH-------- 1329
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLL-TRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAikdAFNnrnveifk 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1330 ---------------------TAVDCCNLAIINSLLRAKANVNIQDSQH-KTPLHYALQRKNMNLVRILVQAGADVNASD 1387
Cdd:PHA02878 119 iiltnrykniqtidlvyidkkSKDDIIEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1388 NNGSSGLHYAVT-YAEPGADAsfeiedfLLKKGANVNKRDNHGRVPLHYAFLKTGNqntpidpIETVSSLcavrdLEIDV 1466
Cdd:PHA02878 199 KTNNSPLHHAVKhYNKPIVHI-------LLENGASTDARDKCGNTPLHISVGYCKD-------YDILKLL-----LEHGV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1467 ADNHKR-----TPLHYAAQRGATTcsLLLLNRKAGLENQDEDGNTPLGLGLK 1513
Cdd:PHA02878 260 DVNAKSyilglTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
853-949 |
1.76e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 853 HYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLEQPSVDVnirDDDGRTLasqLMDIVCESSHK 932
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTA---LHYAARSGHLE 75
|
90
....*....|....*..
gi 470409102 933 QLQYLIEKKsADVTTPD 949
Cdd:pfam12796 76 IVKLLLEKG-ADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1228-1492 |
2.03e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1228 TALHFLVSQPDLL--SDFIHEY-KLDINAQDRKMETplhlAINGDRQDVFNMLLAESSINANVAD--SLGTLPLHLAVNR 1302
Cdd:PHA02878 72 TPLHIICKEPNKLgmKEMIRSInKCSVFYTLVAIKD----AFNNRNVEIFKIILTNRYKNIQTIDlvYIDKKSKDDIIEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1303 QnlaMVDALLQANTDVDKWQR--GRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAG 1380
Cdd:PHA02878 148 E---ITKLLLSYGADINMKDRhkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1381 ADVNASDNNGSSGLHYAVTYAEpgadaSFEIEDFLLKKGANVNKRDN-HGRVPLHYAfLKTgnqntpidpiETVSSLCAV 1459
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVGYCK-----DYDILKLLLEHGVDVNAKSYiLGLTALHSS-IKS----------ERKLKLLLE 288
|
250 260 270
....*....|....*....|....*....|....*
gi 470409102 1460 RDLEIDVADNHKRTPLHYAAQR--GATTCSLLLLN 1492
Cdd:PHA02878 289 YGADINSLNSYKLTPLSSAVKQylCINIGRILISN 323
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
751-908 |
2.04e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 72.36 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQ--PEAVKLLIEKGAHIEAPDVNRMTPLHHaVALGF---VDVAKELVEAGCNIEAADKLKRTAVIHAARN 825
Cdd:PHA03095 154 TPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFkprARIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 826 G---QLVALNYLlrmsaAACCADSSTN----TAAHYAAAFG-WRACLELLVEnGADPNAPNDWKTTPLAIALQKGHLACA 897
Cdd:PHA03095 233 SsckRSLVLPLL-----IAGISINARNrygqTPLHYAAVFNnPRACRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAV 306
|
170
....*....|..
gi 470409102 898 D-FLLEQPSVDV 908
Cdd:PHA03095 307 RaALAKNPSAET 318
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1260-1448 |
3.83e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.18 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1260 TPLHLAINGDRQDVFNMLLAESSI-NANVADSLGtlPLHLAVNRQNLAMVDALLQANTDVDK--WQRGRAALHTAVDCCN 1336
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDvfYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1337 LAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEpgadasFEIEDFLL 1416
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD------IAICKMLL 188
|
170 180 190
....*....|....*....|....*....|..
gi 470409102 1417 KKGANVNKRDNHGRVplhyAFLKTGNQNTPID 1448
Cdd:PHA02875 189 DSGANIDYFGKNGCV----AALCYAIENNKID 216
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
751-1184 |
5.63e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 71.25 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADklkrTAVIHAARNGQLVA 830
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 831 LNYLLRMSAAACCADSSTNTAAHYAA-AFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHlacadflleqpsvdvn 909
Cdd:PHA02876 256 SLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGY---------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 910 iRDDDGRTLASqlmdivcesshkqlqyliekKSADVTTPDTKGLTPLHYVA---QNFDPVQAAAEFKADNDNSD-ADSTS 985
Cdd:PHA02876 320 -DTENIRTLIM--------------------LGADVNAADRLYITPLHQAStldRNKDIVITLLELGANVNARDyCDKTP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 986 PSVNAGKDDMDVDGK--DKGKekgddDKEEVGENDEPKKKKKKTWTNWSVVIaKMLIKHGADVNAQTKDKSTPLMLA-KT 1062
Cdd:PHA02876 379 IHYAAVRNNVVIINTllDYGA-----DIEALSQKIGTALHFALCGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYAcKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1063 RDNEELLILLLDNGAQIAAIHVQDRnvlHQLTPQLMERDLLPLLEAIARNVGEQRFkeMARELDDEGFTpFLRFVQHYGI 1142
Cdd:PHA02876 453 NCKLDVIEMLLDNGADVNAINIQNQ---YPLLIALEYHGIVNILLHYGAELRDSRV--LHKSLNDNMFS-FRYIIAHICI 526
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 470409102 1143 W---SPDHKAKVPSRTKQAPPVVNPEERRRQEKAARDRFRRFLVR 1184
Cdd:PHA02876 527 QdfiRHDIRNEVNPLKRVPTRFTSLRESFKEIIQSDDTFKRIWLR 571
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
931-1390 |
1.15e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 68.06 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 931 HKQLQYLIEKKSADVTTPDTKGLTPLHYVAQNFDPVQAAAEFKADNDNSDADSTSPSVNAGKDDMDVDGKDKGKEKGDDD 1010
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1011 KEEVGENDEPKKKKKKtwtNWSVVIAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAqiaaihvqdrnvl 1090
Cdd:COG0666 81 NAKDDGGNTLLHAAAR---NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1091 hqltpqlmerdllplleaiarnvgeqrfkemarelddegftpflrfvqhygiwspdhkakvpsrtkqappvvnpeerrrq 1170
Cdd:COG0666 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1171 ekaardrfrrflvrfielgavdttapvrstkawrdwkkadpqpkqspgkysltdgrrtalhflvsqpdllsdfiheyklD 1250
Cdd:COG0666 145 -------------------------------------------------------------------------------D 145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1251 INAQDRKMETPLHLAINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVD-KWQRGRAALH 1329
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALD 224
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 470409102 1330 TAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNG 1390
Cdd:COG0666 225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
751-961 |
2.53e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.45 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELV-----------------------EAGCN 807
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktilDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 808 IEAADKLKRTAVIHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAI 887
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 888 ALQKGHLACADFLLEQPSvdvNIRDDDGRTLASQLMDIVCESSHKQLqyLIEKKSADVTtpDTKGLTPLHYVAQ 961
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGN---HIMNKCKNGFTPLHNAIIHNRSAIEL--LINNASINDQ--DIDGSTPLHHAIN 263
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
741-891 |
6.91e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.21 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 741 IDTKSKGSrfTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAV- 819
Cdd:PHA02878 162 MKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLh 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 820 IHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRAcLELLVENGADPNAPNDWKTTPLAIALQK 891
Cdd:PHA02878 240 ISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK-LKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
741-916 |
1.26e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.14 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 741 IDTKSKGSRfTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVI 820
Cdd:PHA02874 117 VNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 821 HAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGwRACLELLVENgADPNAPNDWKTTPLAIALQKghlACA--- 897
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINN-ASINDQDIDGSTPLHHAINP---PCDidi 270
|
170 180
....*....|....*....|
gi 470409102 898 -DFLLEQpSVDVNIRDDDGR 916
Cdd:PHA02874 271 iDILLYH-KADISIKDNKGE 289
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1265-1439 |
2.70e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 65.01 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1265 AINGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVD-KWQRGRAALHTAVDCCNLAIINSL 1343
Cdd:PHA02875 9 AILFGELDIARRLL-DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDvKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1344 LraKANVNIQDSQHK---TPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEpgadasFEIEDFLLKKGA 1420
Cdd:PHA02875 88 L--DLGKFADDVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD------IKGIELLIDHKA 159
|
170
....*....|....*....
gi 470409102 1421 NVNKRDNHGRVPLHYAFLK 1439
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAK 178
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1336-1731 |
9.87e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.53 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1336 NLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEpGADASFEIEDFL 1415
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY-NLTDVKEIVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1416 LKKGANVNKRDNHGRVPLHYAFLKTGNQNTPIDpietvsslcavrdleidvadnhkrtplhyaaqrgattcslLLLNRKA 1495
Cdd:PHA03100 93 LEYGANVNAPDNNGITPLLYAISKKSNSYSIVE----------------------------------------YLLDNGA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1496 GLENQDEDGNTPLGLGLKNGHGDYAIV--LLQKNANVrhpiynvtwgfahdenqrhkrvithstsrsmfyeavsrgwqgv 1573
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESNKIDLKILklLIDKGVDI------------------------------------------- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1574 symmldagldkltaltDAINTgkfqlVVTLLSKtpedevvqgldaddrtlfhhlanycsgkldhwaqtlaekleerGVAM 1653
Cdd:PHA03100 170 ----------------NAKNR-----VNYLLSY-------------------------------------------GVPI 185
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 1654 NVIDKHGRLPLHYASKNGCGVLVDFFLKRSkSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCSALDARVKQKN 1731
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLLYFK 262
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
735-909 |
1.74e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 735 AKLVPY-----IDTKSKGSRF-TALHFAVRNN-QPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALG-FVDVAKELVEAGC 806
Cdd:PHA02876 287 SRLVPKllergADVNAKNIKGeTPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 807 NIEAADKLKRTAVIHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYA-AAFGWRACLELLVENGADPNAPNDWKTTPL 885
Cdd:PHA02876 367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPL 446
|
170 180
....*....|....*....|....*
gi 470409102 886 AIALQKG-HLACADFLLEQpSVDVN 909
Cdd:PHA02876 447 HYACKKNcKLDVIEMLLDN-GADVN 470
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
753-965 |
2.20e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 62.38 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 753 LHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFV-----DVAKELVEAGCNIEAADKLKRTAVIHAARN-- 825
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 826 GQLVALNYLLRMSAAACCADSSTNTAAHYAAafgwRAC------LELLVENGADPNAPNDwkttplaialqkghlacADF 899
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYL----ESNkidlkiLKLLIDKGVDINAKNR-----------------VNY 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 900 LLEQpSVDVNIRDDDGRTlasQLMDIVCESSHKQLQYLIEkKSADVTTPDTKGLTPLHYVAQNFDP 965
Cdd:PHA03100 178 LLSY-GVPINIKDVYGFT---PLHYAVYNNNPEFVKYLLD-LGANPNLVNKYGDTPLHIAILNNNK 238
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1331-1530 |
2.91e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.90 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1331 AVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILV-----------------------QAGADVNASD 1387
Cdd:PHA02874 42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktilDCGIDVNIKD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1388 NNGSSGLHYAVTyaepgaDASFEIEDFLLKKGANVNKRDNHGRVPLHYAFlktgnQNTPIDPIETVSSLCAVrdleIDVA 1467
Cdd:PHA02874 122 AELKTFLHYAIK------KGDLESIKMLFEYGADVNIEDDNGCYPIHIAI-----KHNFFDIIKLLLEKGAY----ANVK 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1468 DNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKngHGDYAIVLLQKNANV 1530
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASI 247
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
848-901 |
3.11e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 3.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 848 TNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLL 901
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1336-1522 |
7.91e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.75 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1336 NLAIINSLLRAKAN-VNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAV---------------- 1398
Cdd:PHA02874 13 DIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIkigahdiikllidngv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1399 -TYAEPGADASFEIEDFLLKKGANVNKRDNHGRVPLHYAfLKTGNqntpidpIETVSSLCAVRdLEIDVADNHKRTPLHY 1477
Cdd:PHA02874 93 dTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYA-IKKGD-------LESIKMLFEYG-ADVNIEDDNGCYPIHI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 470409102 1478 AAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKngHGDYAIV 1522
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE--YGDYACI 206
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1642-1724 |
1.19e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.35 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1642 LAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKrsKSDVNLIDeNGKSPLVYAVLGSHLQVAERLMARKADCS 1721
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
|
...
gi 470409102 1722 ALD 1724
Cdd:pfam12796 89 VKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
751-802 |
2.27e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 2.27e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELV 802
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1035-1374 |
4.03e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.50 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLI-LLLDNGAQIAAIHVQDRNVLH-QLTPQLMERDLLPLLeaIARN 1112
Cdd:PHA03095 65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGRTPLHvYLSGFNINPKVIRLL--LRKG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1113 VGeqrfkemARELDDEGFTP---FLRFVQhygiwspdhkakvpsrtkqappvVNPEerrrqekaardrfrrfLVRF-IEL 1188
Cdd:PHA03095 143 AD-------VNALDLYGMTPlavLLKSRN-----------------------ANVE----------------LLRLlIDA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1189 GAVDTTAPVRstkawrdwkkadpqpkqspgkysltdgRRTALH-FLVS---QPDLLSDFIhEYKLDINAQDRKMETPLHL 1264
Cdd:PHA03095 177 GADVYAVDDR---------------------------FRSLLHhHLQSfkpRARIVRELI-RAGCDPAATDMLGNTPLHS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1265 AINGD---RQDVFNMLLAESSINANvaDSLGTLPLHLAVNRQNlamvdallqantdvdkwqrgraalHTAVDCcnlaiin 1341
Cdd:PHA03095 229 MATGSsckRSLVLPLLIAGISINAR--NRYGQTPLHYAAVFNN------------------------PRACRR------- 275
|
330 340 350
....*....|....*....|....*....|...
gi 470409102 1342 sLLRAKANVNIQDSQHKTPLHYALQRKNMNLVR 1374
Cdd:PHA03095 276 -LIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1394-1501 |
5.99e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.43 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1394 LHYAVtyaepgADASFEIEDFLLKKGANVNKRDNHGRVPLHYAfLKTGNqntpidpIETVSSLCAVRDLEIDvadNHKRT 1473
Cdd:pfam12796 1 LHLAA------KNGNLELVKLLLENGADANLQDKNGRTALHLA-AKNGH-------LEIVKLLLEHADVNLK---DNGRT 63
|
90 100
....*....|....*....|....*...
gi 470409102 1474 PLHYAAQRGATTCSLLLLNRKAGLENQD 1501
Cdd:pfam12796 64 ALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
1325-1532 |
7.33e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1325 RAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEPG 1404
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1405 A-----DASFEIEDFLLKKGanvnkrdnhgRVPLHYAflktgnqnTPIDPIETVSSLCAvRDLEIDVADNHKRTPLHYAA 1479
Cdd:PHA02875 83 AveellDLGKFADDVFYKDG----------MTPLHLA--------TILKKLDIMKLLIA-RGADPDIPNTDKFSPLHLAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1480 QRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANVRH 1532
Cdd:PHA02875 144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1463-1530 |
9.03e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 9.03e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 1463 EIDVADNHKRTPLHYAAQRGATTCSLLLLNRKAGleNQDEDGNTPLGLGLKNGHGDYAIVLLQKNANV 1530
Cdd:pfam12796 22 DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1268-1494 |
1.50e-07 |
|
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: 57.01 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1268 GDRQDVFNMLLAESSINANVADSLGTLPLHLAVNR-QNLAMVDALLQANTDVDKwqrGRAALHTA----VDCCNLAIINS 1342
Cdd:TIGR00870 28 GDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIEnENLELTELLLNLSCRGAV---GDTLLHAIsleyVDAVEAILLHL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1343 LLRAKANVNIQ---DSQ------HKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTYAEPG--------A 1405
Cdd:TIGR00870 105 LAAFRKSGPLElanDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGVDSFYHGesplnaaaC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1406 DASFEIEDFLLKKGANVNKRDNHGRVPLHYAFLKTGNQNtpiDPIETVSS-----------LCAVRDLEIDVadNHK-RT 1473
Cdd:TIGR00870 185 LGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKA---EYEELSCQmynfalslldkLRDSKELEVIL--NHQgLT 259
|
250 260
....*....|....*....|.
gi 470409102 1474 PLHYAAQRGATTCSLLLLNRK 1494
Cdd:TIGR00870 260 PLKLAAKEGRIVLFRLKLAIK 280
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1294-1494 |
1.71e-07 |
|
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: 56.56 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1294 LPLHLAVNRQNLAMVDALLQANtDVDKWQRG---RAALHTAVDCCNLAIINSLLRAK---ANVNIQDS--QHKTPLHYAL 1365
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGalgETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1366 QRKNMNLVRILVQAGADVNASDNNGssglhyavTYAEPGADA---------SF-------EIEDFLLKKGANVNKRDNHG 1429
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSPRATG--------TFFRPGPKNliyygehplSFaacvgneEIVRLLIEHGADIRAQDSLG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 1430 RVPLHYAFLKTgNQNTPIDPIETVSSLCA-VRDLEIDVADNHK-RTPLHYAAQRGATTCSLLLLNRK 1494
Cdd:cd22192 170 NTVLHILVLQP-NKTFACQMYDLILSYDKeDDLQPLDLVPNNQgLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
750-813 |
3.10e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 55.44 E-value: 3.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 750 FTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADK 813
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1620-1925 |
3.85e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1620 DRTLFHHLANYCSGKLDHWAQTLAEKleerGVAMNVIDKHGRLPLHYASKNGCGV-LVDFFLKRsKSDVNLIDENGKSPL 1698
Cdd:PHA03095 47 GKTPLHLYLHYSSEKVKDIVRLLLEA----GADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA-GADVNAKDKVGRTPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1699 -VY-AVLGSHLQVAERLMARKADCSALDArvkqknqaHGRhnTPekkqrrhakAAAALSKVAQETHLVIYAMRASladll 1776
Cdd:PHA03095 122 hVYlSGFNINPKVIRLLLRKGADVNALDL--------YGM--TP---------LAVLLKSRNANVELLRLLIDAG----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1777 nlllankADLNAKDSLGNTCLIYavrnndtdmvHLLFTKRRgaakpgpssssssssappsslspaePELMLEN-ETGIDP 1855
Cdd:PHA03095 178 -------ADVYAVDDRFRSLLHH----------HLQSFKPR-------------------------ARIVRELiRAGCDP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1856 NVQDEQGKTALHHvvspLDYGSYENVALLTMLLKAGADPNVKDNQGHTPLYYALQQRDGVMAARLRSLGA 1925
Cdd:PHA03095 216 AATDMLGNTPLHS----MATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
782-835 |
4.17e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 4.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 782 RMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVALNYLL 835
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1230-1319 |
4.61e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 49.73 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1230 LHFLVSQPDLLS-DFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSINanvADSLGTLPLHLAVNRQNLAMV 1308
Cdd:pfam12796 1 LHLAAKNGNLELvKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 470409102 1309 DALLQANTDVD 1319
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
660-836 |
4.74e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 55.06 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 660 LKLLLDRGVSHREVDREGSTSLMIAAQC--GRLDSIKLLLDwdsrkmaeaekeaeesdkehssdddeeeeaprkqpRAkl 737
Cdd:PHA03100 89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-----------------------------------NG-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 738 vpyIDTKSKGSR-FTALHFAVRNNQPE------------------AVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVA 798
Cdd:PHA03100 132 ---ANVNIKNSDgENLLHLYLESNKIDlkilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 470409102 799 KELVEAGCNIEAADKLKRTAVIHAARNGQLVALNYLLR 836
Cdd:PHA03100 209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
1642-1928 |
7.92e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 54.68 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1642 LAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRSkSDVNLIDENGKSPLVYAVLGSHLQ-----VAERLMAR 1716
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDtikaiIDNRSNIN 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1717 KADCSALDARVKQK--------------NQAHGRHNTPekkqRRHAKAAAALSKVAQEThlviyamrasladllnllLAN 1782
Cdd:PHA02876 239 KNDLSLLKAIRNEDletslllydagfsvNSIDDCKNTP----LHHASQAPSLSRLVPKL------------------LER 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1783 KADLNAKDSLGNTCLIYAVRNN-DTDMVHLLFTKrrgaakpgpssssssssappsslspaepelmlenetGIDPNVQDEQ 1861
Cdd:PHA02876 297 GADVNAKNIKGETPLYLMAKNGyDTENIRTLIML------------------------------------GADVNAADRL 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 470409102 1862 GKTALHHvVSPLDygsyENVALLTMLLKAGADPNVKDNQGHTPLYYALQQRDGVMAARLRSLGAKLD 1928
Cdd:PHA02876 341 YITPLHQ-ASTLD----RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1657-1908 |
1.22e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.52 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1657 DKHGRLPLHYASKNGCGVLVDFFLKRSKsDVNLIDENGKSPLVY-----AVLGSHLQVAERLMARKADCSALDARvkqkn 1731
Cdd:PHA03100 32 YKKPVLPLYLAKEARNIDVVKILLDNGA-DINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNN----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1732 qahgrHNTPekkqrrhakAAAALSKVAQETHLVIYamrasladllnlLLANKADLNAKDSLGNTCLIYAVRNN--DTDMV 1809
Cdd:PHA03100 106 -----GITP---------LLYAISKKSNSYSIVEY------------LLDNGANVNIKNSDGENLLHLYLESNkiDLKIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1810 HLLFTKrrGA---AKpgpssssssssappsslspAEPELMLENetGIDPNVQDEQGKTALHHVVSpldygsYENVALLTM 1886
Cdd:PHA03100 160 KLLIDK--GVdinAK-------------------NRVNYLLSY--GVPINIKDVYGFTPLHYAVY------NNNPEFVKY 210
|
250 260
....*....|....*....|..
gi 470409102 1887 LLKAGADPNVKDNQGHTPLYYA 1908
Cdd:PHA03100 211 LLDLGANPNLVNKYGDTPLHIA 232
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1308-1532 |
1.80e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.72 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1308 VDALLQANTDVDKWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASD 1387
Cdd:PLN03192 509 VGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1388 NNGSSGLHYAVtyaepgADASFEIEDFLlkkganvnkrdnhgrvplhYAFLKTGNQNTPIDpietvsSLCavrdleidva 1467
Cdd:PLN03192 589 ANGNTALWNAI------SAKHHKIFRIL-------------------YHFASISDPHAAGD------LLC---------- 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470409102 1468 dnhkrtplhYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLQKNANVRH 1532
Cdd:PLN03192 628 ---------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1797-1930 |
1.92e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.19 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1797 LIYAVRNNDTDMVHLLFtkrrgaakpgpssssssssappsslspaepelmlenETGIDPNVQDEQGKTALHHVVSpldYG 1876
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL------------------------------------ENGADANLQDKNGRTALHLAAK---NG 41
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1877 SYENValltMLLKAGADPNVKDNqGHTPLYYALQQRDGVMAARLRSLGAKLDKK 1930
Cdd:pfam12796 42 HLEIV----KLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
1328-1438 |
2.09e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 50.97 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1328 LHTAVD--CCNLAIINSLLRAKANVN-IQDSQHKTPLHYALQ-RKNMN--LVRILVQAGADVNASDNNGSSGLHYAVTya 1401
Cdd:PHA02859 55 IFSCLEkdKVNVEILKFLIENGADVNfKTRDNNLSALHHYLSfNKNVEpeILKILIDSGSSITEEDEDGKNLLHMYMC-- 132
|
90 100 110
....*....|....*....|....*....|....*..
gi 470409102 1402 epGADASFEIEDFLLKKGANVNKRDNHGRVPLHYAFL 1438
Cdd:PHA02859 133 --NFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYIL 167
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1035-1319 |
3.92e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.97 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPLMLAKT-----RDNEELLILLLDNGAQIAAIhvqDRNVLHQLTPQLMER----DLLPL 1105
Cdd:PHA03100 50 VVKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAP---DNNGITPLLYAISKKsnsySIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1106 LEAIARNVgeqrfkemaRELDDEGFTPFlrfvqHYGIWSPDHKAKVpsrtkqappvvnpeerrrqekaardrfRRFLVRf 1185
Cdd:PHA03100 127 LLDNGANV---------NIKNSDGENLL-----HLYLESNKIDLKI---------------------------LKLLID- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1186 ielgavdttapvrstkawrdwKKADpqpkqspgkysltdgrrtalhflVSQPDLLSDFIhEYKLDINAQDRKMETPLHLA 1265
Cdd:PHA03100 165 ---------------------KGVD-----------------------INAKNRVNYLL-SYGVPINIKDVYGFTPLHYA 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1266 INGDRQDVFNMLLaESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVD 1319
Cdd:PHA03100 200 VYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1259-1416 |
3.98e-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: 52.32 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1259 ETPLHLAINGDRQDVFNMLLAESS--INANVADSL--GTLPLHLAVNRQNLAMVDALLQANTDVdkwQRGRAalhtavdc 1334
Cdd:cd22192 52 ETALHVAALYDNLEAAVVLMEAAPelVNEPMTSDLyqGETALHIAVVNQNLNLVRELIARGADV---VSPRA-------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1335 CNLAiinsLLRAKANVnIQDSQHktPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVTyaEPGADASFEIEDF 1414
Cdd:cd22192 121 TGTF----FRPGPKNL-IYYGEH--PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL--QPNKTFACQMYDL 191
|
..
gi 470409102 1415 LL 1416
Cdd:cd22192 192 IL 193
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1248-1387 |
4.65e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1248 KLDINAQDRKMETPLHLAINGDRQDVFnMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKwQRGRAA 1327
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDCV-LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP-HAAGDL 625
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1328 LHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASD 1387
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| WGR |
cd07994 |
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ... |
2030-2092 |
7.82e-06 |
|
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain.
Pssm-ID: 153424 Cd Length: 73 Bit Score: 45.73 E-value: 7.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 2030 GINNFYKMQVIHNKLKDFYILWTRWGRIGDV-GQYQRTPFPTAEATVEEFKKIFKAKTGNSWED 2092
Cdd:cd07994 10 GSNKYYKLQLLEDDKENRYWVFRSYGRVGTViGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1359-1398 |
1.02e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 470409102 1359 TPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAV 1398
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
865-1091 |
1.19e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.83 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 865 ELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLEQpSVDVNIRDDDGRTLASQLMD---------IVCESSH---K 932
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDsknidtikaIIDNRSNinkN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 933 QLQYLIEKKSADVTTP-------------DTKGLTPLHYVAQNfdP-----VQAAAEFKADNDNSDADSTSPSVNAGKDD 994
Cdd:PHA02876 241 DLSLLKAIRNEDLETSlllydagfsvnsiDDCKNTPLHHASQA--PslsrlVPKLLERGADVNAKNIKGETPLYLMAKNG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 995 MDVDGKDKGKEKGDDDKEEVGENDEPKKKKKKTWTNWSVVIAkmLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLD 1074
Cdd:PHA02876 319 YDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250
....*....|....*..
gi 470409102 1075 NGAQIAAIHVQDRNVLH 1091
Cdd:PHA02876 397 YGADIEALSQKIGTALH 413
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
734-915 |
1.22e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.02 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 734 RAKLVPYIdTKSKGSrfTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVE--AGCNIEAA 811
Cdd:PLN03192 546 KAKLDPDI-GDSKGR--TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHAA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 812 DKLkrtaVIHAARNGQLVALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGAD---PNAPNDWKTTPLAIA 888
Cdd:PLN03192 623 GDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSPTELREL 698
|
170 180
....*....|....*....|....*..
gi 470409102 889 LQKGHLACADFLLEQPSVDVNIRDDDG 915
Cdd:PLN03192 699 LQKRELGHSITIVDSVPADEPDLGRDG 725
|
|
| WGR_MMR_like |
cd07996 |
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ... |
2027-2086 |
1.46e-05 |
|
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain.
Pssm-ID: 153425 Cd Length: 74 Bit Score: 44.90 E-value: 1.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2027 GTHGINNFYKMQVIHNkLKDFYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKT 2086
Cdd:cd07996 9 PERNSARFYEIELEGD-LFGEWSLVRRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKL 67
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1646-1701 |
1.88e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 1646 LEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRsKSDVNLIDENGKSPLVYA 1701
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
|
|
| tankyrase_like |
cd01438 |
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ... |
2387-2509 |
2.75e-05 |
|
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).
Pssm-ID: 238718 [Multi-domain] Cd Length: 223 Bit Score: 47.97 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 2387 HLQRKGEPERFqerweKVPNHQLLFHGSALSNfvGILSQGL--RIAppeapFSGYAFGKGIYFADMFQKS--FGYCRMGH 2462
Cdd:cd01438 74 HRQKEIAEENH-----NHHNERMLFHGSPFIN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSnqYVYGIGGG 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 2463 TGSrhsqPERKNTGF------MLMCEVALGEMNAITQAEYMEKAPQGFHSTKG 2509
Cdd:cd01438 142 TGC----PTHKDRSCyvchrqMLFCRVTLGKSFLQFSAMKMAHAPPGHHSVIG 190
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
1349-1482 |
3.23e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 49.42 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1349 NVNIQDSQHK--TPLHYALQRKNMNLVRILVQAGADVNASdnngSSGLHYAVTYAEPG------------ADASFEIEDF 1414
Cdd:cd22196 84 NAAYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHAR----ASGEFFKKKKGGPGfyfgelplslaaCTNQLDIVKF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1415 LLK---KGANVNKRDNHGRVPLH------------YAF--------LKTGNQNTPIDPIEtvsslcavrdleiDVADNHK 1471
Cdd:cd22196 160 LLEnphSPADISARDSMGNTVLHalvevadntpenTKFvtkmyneiLILGAKIRPLLKLE-------------EITNKKG 226
|
170
....*....|.
gi 470409102 1472 RTPLHYAAQRG 1482
Cdd:cd22196 227 LTPLKLAAKTG 237
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
750-986 |
3.32e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 750 FTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLH----HAVALGFVDVAKELVEagCNIEAADKLKRTA------- 818
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickEPNKLGMKEMIRSINK--CSVFYTLVAIKDAfnnrnve 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 819 -----VIHAARNGQLVALNY-----------------LLRMSAAACCADSST-NTAAHYAAAFGWRACLELLVENGADPN 875
Cdd:PHA02878 116 ifkiiLTNRYKNIQTIDLVYidkkskddiieaeitklLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 876 APNDWKTTPLAIALQKGHLACADFLLEQPSvDVNIRDDDGRT----LASQLMDIvcesshKQLQYLIEKkSADVTTPDT- 950
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGA-STDARDKCGNTplhiSVGYCKDY------DILKLLLEH-GVDVNAKSYi 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 470409102 951 KGLTPLHYVAQNFDPVQAAAEFKADNDNSDADSTSP 986
Cdd:PHA02878 268 LGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTP 303
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
907-1093 |
3.42e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.87 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 907 DVNIRDDDGRTLASQLMDIVCESSHKQLQYLIEKkSADVTTPDTKGLTPLHYVAQN---FDPVQAAAEFKAD-NDNSDAD 982
Cdd:PHA03095 39 DVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEA-GADVNAPERCGFTPLHLYLYNattLDVIKLLIKAGADvNAKDKVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 983 STSPSVNAgkddmdvdgkdKGKekgdddkeevgendepkkkkkktWTNWSVViaKMLIKHGADVNAQTKDKSTPL--MLA 1060
Cdd:PHA03095 118 RTPLHVYL-----------SGF-----------------------NINPKVI--RLLLRKGADVNALDLYGMTPLavLLK 161
|
170 180 190
....*....|....*....|....*....|...
gi 470409102 1061 KTRDNEELLILLLDNGAQIAAIHVQDRNVLHQL 1093
Cdd:PHA03095 162 SRNANVELLRLLIDAGADVYAVDDRFRSLLHHH 194
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1784-1898 |
3.55e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 44.34 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1784 ADLNAKDSLGNTCLIYAVRNNDTDMVhllftkrrgaakpgpssssssssappsslspaepELMLENetgIDPNVQDEqGK 1863
Cdd:pfam12796 21 ADANLQDKNGRTALHLAAKNGHLEIV----------------------------------KLLLEH---ADVNLKDN-GR 62
|
90 100 110
....*....|....*....|....*....|....*
gi 470409102 1864 TALHHVVSpldYGSYENVALltmLLKAGADPNVKD 1898
Cdd:pfam12796 63 TALHYAAR---SGHLEIVKL---LLEKGADINVKD 91
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
867-918 |
3.56e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 3.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 867 LVENG-ADPNAPNDWKTTPLAIALQKGHLACADFLLEQPsVDVNIRDDDGRTL 918
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTA 52
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
750-902 |
3.98e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.83 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 750 FTALHFAVRNNQPEAVKLLIEKGAH--IEAPDVNrmTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQ 827
Cdd:PHA02875 36 ISPIKLAMKFRDSEAIKLLMKHGAIpdVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 828 LV-ALNYLLRMSAAACCADSSTNTAAHYAAAFGWRACLELLVENGADPNAPNDWKTTPLAIALQKGHLACADFLLE 902
Cdd:PHA02875 114 KLdIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1462-1583 |
5.33e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.71 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1462 LEIDVADNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHgdyaivllqknanvrHPIYNVTWGF 1541
Cdd:PLN03192 549 LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH---------------HKIFRILYHF 613
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 470409102 1542 AHDENQRhkrvithsTSRSMFYEAVSRGWQGVSYMMLDAGLD 1583
Cdd:PLN03192 614 ASISDPH--------AAGDLLCTAAKRNDLTAMKELLKQGLN 647
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1846-1908 |
6.42e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 6.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1846 MLENETgIDPNVQDEQGKTALHHVVSpldYGSYENVAlltMLLKAGADPNVKDNQGHTPLYYA 1908
Cdd:pfam13857 1 LLEHGP-IDLNRLDGEGYTPLHVAAK---YGALEIVR---VLLAYGVDLNLKDEEGLTALDLA 56
|
|
| WGR |
COG3831 |
WGR domain, predicted DNA-binding domain in MolR [Transcription]; |
2034-2086 |
7.35e-05 |
|
WGR domain, predicted DNA-binding domain in MolR [Transcription];
Pssm-ID: 443043 Cd Length: 83 Bit Score: 43.44 E-value: 7.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 2034 FYKMQVIHNKLKDfYILWTRWGRIGDVGQYQRTPFPTAEATVEEFKKIFKAKT 2086
Cdd:COG3831 17 FYELEVEPDLFGG-WSLTRRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKL 68
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1356-1385 |
7.37e-05 |
|
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: 41.80 E-value: 7.37e-05
10 20 30
....*....|....*....|....*....|
gi 470409102 1356 QHKTPLHYALQRKNMNLVRILVQAGADVNA 1385
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1664-1715 |
7.53e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.57 E-value: 7.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1664 LHYASKNGCGVLVDFFLKrSKSDVNLIDENGKSPLVYAVLGSHLQVAERLMA 1715
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1348-1397 |
8.20e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 8.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 470409102 1348 ANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYA 1397
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1619-1812 |
8.39e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 47.74 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1619 DDRTLFHHLANYCSGKLDhwAQTLAEKLEERGVAMNVIDKHGRLPLHYASKNGCG--VLVDFFLKRSKsDVNLIDENGKS 1696
Cdd:PHA03100 67 NNSTPLHYLSNIKYNLTD--VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNsySIVEYLLDNGA-NVNIKNSDGEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1697 PLVYAVLGSH--LQVAERLMARKADCSALDaRVK-------QKNQAHGRHNTPekkqrrhakaaaalskvaqethlVIYA 1767
Cdd:PHA03100 144 LLHLYLESNKidLKILKLLIDKGVDINAKN-RVNyllsygvPINIKDVYGFTP-----------------------LHYA 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 470409102 1768 MRASLADLLNLLLANKADLNAKDSLGNTCLIYAVRNNDTDMVHLL 1812
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1324-1377 |
9.86e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 9.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1324 GRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILV 1377
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1475-1538 |
1.31e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.80 E-value: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1475 LHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLLqKNANVRHPIYNVT 1538
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGRT 63
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1035-1098 |
1.48e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.80 E-value: 1.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPLMLAKTRDNEELLILLLDNGAQiaaihvqdRNVLHQLTPqLM 1098
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--------NLKDNGRTA-LH 66
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1359-1388 |
1.59e-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: 40.74 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|.
gi 470409102 1359 TPLHYA-LQRKNMNLVRILVQAGADVNASDN 1388
Cdd:pfam00023 4 TPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1244-1299 |
1.60e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 1244 IHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLLAESSiNANVADSLGTLPLHLA 1299
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1641-1909 |
1.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 46.88 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1641 TLAEKL-EERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKrSKSDVNLIDENGKSPLVYAV-LGSHlQVAERLMARKA 1718
Cdd:PHA02874 15 EAIEKIiKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIK-HGADINHINTKIPHPLLTAIkIGAH-DIIKLLIDNGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1719 DCSALDARVKQKNQAHGRHNTPEKKQRRHAKAAAALSkvaqethlviYAMRASLADLLNLLLANKADLNAKDSLGNTCLI 1798
Cdd:PHA02874 93 DTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLH----------YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1799 YAVRNNDTDMVHLLFtkrrgaakpgpssssssssappsslspaepelmlenETGIDPNVQDEQGKTALHHVVsplDYGSY 1878
Cdd:PHA02874 163 IAIKHNFFDIIKLLL------------------------------------EKGAYANVKDNNGESPLHNAA---EYGDY 203
|
250 260 270
....*....|....*....|....*....|.
gi 470409102 1879 ENVALltmLLKAGADPNVKDNQGHTPLYYAL 1909
Cdd:PHA02874 204 ACIKL---LIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1460-1508 |
1.73e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 470409102 1460 RDLEIDVADNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPL 1508
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1376-1436 |
1.82e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1376 LVQAG-ADVNASDNNGSSGLHYAVTYAepgadaSFEIEDFLLKKGANVNKRDNHGRVPLHYA 1436
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYG------ALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1784-1913 |
1.84e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.80 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1784 ADLNAKD-SLGNTCLIYAVRNNDTDMVHLLFTKrrgAAKPGPSSSSSSSSAPPSSLSPAEP--ELMLENetGIDPNVQDE 1860
Cdd:PHA02878 158 ADINMKDrHKGNTALHYATENKDQRLTELLLSY---GANVNIPDKTNNSPLHHAVKHYNKPivHILLEN--GASTDARDK 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1861 QGKTALHHVVspldyGSYENVALLTMLLKAGADPNVKDN-QGHTPLYYALQQRD 1913
Cdd:PHA02878 233 CGNTPLHISV-----GYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER 281
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
1295-1429 |
1.94e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.20 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1295 PLHLAVNRQ--NLAMVDALLQANTDVDKWQRGR--AALH---TAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYALQR 1367
Cdd:PHA02859 54 PIFSCLEKDkvNVEILKFLIENGADVNFKTRDNnlSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCN 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1368 KNMNL--VRILVQAGADVNASDNNGSSGLHYAVTYAEPGadasfEIEDFLLKKGANVNKRDNHG 1429
Cdd:PHA02859 134 FNVRInvIKLLIDSGVSFLNKDFDNNNILYSYILFHSDK-----KIFDFLTSLGIDINETNKSG 192
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1286-1508 |
2.34e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.20 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1286 NVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKWQRGRAalHTAVDCCNLAIINSLLRAKANVNIQDSQHKTPLHYAL 1365
Cdd:PHA02946 3 NIMSAEYYLSLYAKYNSKNLDVFRNMLQAIEPSGNYHILHA--YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1366 QRKNMNLVRILVQAGADVNASDNNGSSGLHyavtYAEPGADASFEIEDFLLKKGANVNKR-DNHGRVPLHYAflktgnqn 1444
Cdd:PHA02946 81 KINNNRIVAMLLTHGADPNACDKQHKTPLY----YLSGTDDEVIERINLLVQYGAKINNSvDEEGCGPLLAC-------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 1445 tpIDPIETVSSLCAVRDLEIDVADNHKRTPLHYAAQRGATTCSLLLLNRKAGL--ENQDEDGNTPL 1508
Cdd:PHA02946 149 --TDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGIspSKPDHDGNTPL 212
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
751-821 |
2.58e-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: 46.54 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPdvnRMT-----------------PLHHAVALGFVDVAKELVEAGCNIEAADK 813
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
|
....*...
gi 470409102 814 LKRTaVIH 821
Cdd:cd22192 168 LGNT-VLH 174
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1358-1493 |
2.72e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 46.29 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1358 KTPLHYALQRKNMNLVRILVQAGADVNA---------SDNN-----GSSGLHYAVTYAEPgadasfEIEDFLLKKGA-NV 1422
Cdd:cd22194 142 QTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQP------EIVQLLMEKEStDI 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470409102 1423 NKRDNHGRVPLHYAFLKTGNQNTPIDPI----ETVSSLCAVRDLEiDVADNHKRTPLHYAAQRGATTCSLLLLNR 1493
Cdd:cd22194 216 TSQDSRGNTVLHALVTVAEDSKTQNDFVkrmyDMILLKSENKNLE-TIRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1472-1524 |
3.58e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 3.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 470409102 1472 RTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLL 1524
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
725-823 |
4.63e-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: 45.84 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 725 EEEAPRKQPRAKLV--PYIDTKSKGSrfTALHFAVRNNQPEAVKLLIEKGAHIEA----------PDVNRM----TPLHH 788
Cdd:TIGR00870 104 LLAAFRKSGPLELAndQYTSEFTPGI--TALHLAAHRQNYEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNA 181
|
90 100 110
....*....|....*....|....*....|....*
gi 470409102 789 AVALGFVDVAKELVEAGCNIEAADKLKRTaVIHAA 823
Cdd:TIGR00870 182 AACLGSPSIVALLSEDPADILTADSLGNT-LLHLL 215
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
751-777 |
4.96e-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.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.55 E-value: 4.96e-04
10 20
....*....|....*....|....*..
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEA 777
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
747-789 |
5.31e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 5.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 470409102 747 GSRFTALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHA 789
Cdd:pfam13857 14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1035-1082 |
6.24e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 44.83 E-value: 6.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 470409102 1035 IAKMLIKHGADVNAQTKDKSTPL--MLA-KTRDNEELLILLLDNGAQIAAI 1082
Cdd:PHA02798 91 IVKILIENGADINKKNSDGETPLycLLSnGYINNLEILLFMIENGADTTLL 141
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1465-1524 |
8.17e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 8.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1465 DVADNHKRTPLHYAAQRGATTCSLLLLNRKAGLENQDEDGNTPLGLGLKNGHGDYAIVLL 1524
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1646-1728 |
8.90e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1646 LEERGVAMNVIDKHGRLPLHYASKNG----CGVLVDFflkrsKSDVNLIDENGKSPLVYAVLGSHLQVAERLMARKADCS 1721
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGhvqvVRVLLEF-----GADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
....*..
gi 470409102 1722 ALDARVK 1728
Cdd:PTZ00322 176 ELGANAK 182
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
741-813 |
9.81e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.88 E-value: 9.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470409102 741 IDTKSKGSRFTALHFAV---RNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVAlGF---VDVAKELVEAGCNIEAADK 813
Cdd:PHA02859 79 VNFKTRDNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC-NFnvrINVIKLLIDSGVSFLNKDF 156
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1278-1428 |
1.13e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.47 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1278 LAESSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVD-KWQRGRAALHTAVDCCNLAIINSLLRAKANVNIQDSq 1356
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHiRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA- 622
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 470409102 1357 hKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAVtyAEPGADASfeieDFLLKKGANVNKRDNH 1428
Cdd:PLN03192 623 -GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM--AEDHVDMV----RLLIMNGADVDKANTD 687
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
751-875 |
1.22e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.83 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 751 TALHFAVRNNQPEAVKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNGQLVA 830
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 470409102 831 LNYLLrmsaaaccaDSSTN----------TAAHYAAAFGWRACLELLVENGADPN 875
Cdd:PHA02875 184 CKMLL---------DSGANidyfgkngcvAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1660-1713 |
1.26e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1660 GRLPLHYASKNGCGVLVDFFLKrSKSDVNLIDENGKSPLVYAVLGSHLQVAERL 1713
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
1356-1494 |
1.40e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 44.10 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1356 QHKTPLHYALQRKNMNLVRILVQAGADVNASDN------NGSSGLHYA---VTYAepGADASFEIEDFLLKKG---ANVN 1423
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkSPGNLFYFGelpLSLA--ACTNQEEIVRLLLENGaqpAALE 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 1424 KRDNHGRVPLHYAFLKTGNQNTPIDPIETVSSLCAVRD------LEIDVADNHK-RTPLHYAAQRGATTCSLLLLNRK 1494
Cdd:cd21882 150 AQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGahldptQQLEEIPNHQgLTPLKLAAVEGKIVMFQHILQRE 227
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1850-1910 |
1.45e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 43.80 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 470409102 1850 ETGIDPNVQDEQGKTALHHVVSPLDYGSyenvalLTMLLKAGADPNVKDNQGHTPLYYALQ 1910
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLES------IKMLFEYGADVNIEDDNGCYPIHIAIK 166
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
1246-1315 |
1.48e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 41.40 E-value: 1.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 470409102 1246 EYKLDINAQDRKM-ETPLHLAINGDRQDVFNMLLAESSINANVADSLGTLPLHLAVNRQNLAMVDaLLQAN 1315
Cdd:PHA02736 79 EWGADINGKERVFgNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMN-ILRAK 148
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
850-961 |
1.70e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.59 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 850 TAAHYAAAfgwRACLE---LLVENGADPNA--------PND------WKTTPLAIALQKGHLACADFLLEQPSVDVNIRD 912
Cdd:cd22194 143 TALNIAIE---RRQGDivkLLIAKGADVNAhakgvffnPKYkhegfyFGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 913 DDGRTLASQLMdIVCESSHKQLQYLIE------KKSADV---TTPDTKGLTPLHYVAQ 961
Cdd:cd22194 220 SRGNTVLHALV-TVAEDSKTQNDFVKRmydmilLKSENKnleTIRNNEGLTPLQLAAK 276
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
781-813 |
1.91e-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: 38.04 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|....
gi 470409102 781 NRMTPLHHAVA-LGFVDVAKELVEAGCNIEAADK 813
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
1030-1091 |
1.92e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 470409102 1030 NWSVVIAKMLIKHGADVNAQTKDKSTPLM---LAKTRD-NEELLILLLDNGAQIAAIHVQDRNVLH 1091
Cdd:PHA02859 63 KVNVEILKFLIENGADVNFKTRDNNLSALhhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLH 128
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1331-1398 |
2.32e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 43.35 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1331 AVDCCNLAI------INSLLRAKANVNIQDSQHKTPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAV 1398
Cdd:PTZ00322 83 TVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1226-1278 |
2.41e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 2.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 470409102 1226 RRTALHFLVSQPDLLS-DFIHEYKLDINAQDRKMETPLHLAINGDRQDVFNMLL 1278
Cdd:pfam13637 1 ELTALHAAAASGHLELlRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
750-779 |
2.62e-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: 37.65 E-value: 2.62e-03
10 20 30
....*....|....*....|....*....|.
gi 470409102 750 FTALHFAV-RNNQPEAVKLLIEKGAHIEAPD 779
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1624-1713 |
3.29e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.73 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1624 FHHLANYCSGK-LDhwaQTLAEKLEERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKRSkSDVNLIDENGKSPLVYaV 1702
Cdd:PHA02946 38 YHILHAYCGIKgLD---ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHG-ADPNACDKQHKTPLYY-L 112
|
90
....*....|.
gi 470409102 1703 LGSHLQVAERL 1713
Cdd:PHA02946 113 SGTDDEVIERI 123
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
1324-1398 |
3.33e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 41.95 E-value: 3.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470409102 1324 GRAALHTAVDCCNLAIINSLLRAKANVNIQDSQHktPLHYALQRKNMNLVRILVQAGADVNASDNNGSSGLHYAV 1398
Cdd:PHA02791 30 GHSALYYAIADNNVRLVCTLLNAGALKNLLENEF--PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1783-1812 |
3.51e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|
gi 470409102 1783 KADLNAKDSLGNTCLIYAVRNNDTDMVHLL 1812
Cdd:pfam13637 24 GADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
765-847 |
4.06e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 765 VKLLIEKGAHIEAPDVNRMTPLHHAVALGFVDVAKELVEAGCNIEAADKLKRTAVIHAARNG-----QLVALNYLLRMSA 839
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrevvQLLSRHSQCHFEL 177
|
....*...
gi 470409102 840 AACCADSS 847
Cdd:PTZ00322 178 GANAKPDS 185
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
750-777 |
4.09e-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: 36.80 E-value: 4.09e-03
10 20
....*....|....*....|....*...
gi 470409102 750 FTALHFAVRNNQPEAVKLLIEKGAHIEA 777
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
1250-1433 |
4.16e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 42.59 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1250 DINAQDRKMETPLHLAINGDR--QDVFNMLLaESSINANVADSLGTLP-LHLAVNRQNL-AMVDALLQANTDVDKWQRGR 1325
Cdd:PHA02716 204 NVNLQNNHLITPLHTYLITGNvcASVIKKII-ELGGDMDMKCVNGMSPiMTYIINIDNInPEITNIYIESLDGNKVKNIP 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1326 AALHTAVDCC---NLAIINSLLRAKANVNIQDSQHKTPLHYALQRKNMN--LVRILVQAGADVNASDNNGSSGLHY---- 1396
Cdd:PHA02716 283 MILHSYITLArniDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHTylsm 362
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 470409102 1397 --AVTYAEPGADASFEIE--DFLLKKGANVNKRDNHGRVPL 1433
Cdd:PHA02716 363 lsVVNILDPETDNDIRLDviQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
1341-1482 |
4.16e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 42.48 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1341 NSLLRAKANVNIQDSQHK--TPLHYALQRKNMNLVRILVQAGADVNASDNngssGLHYAVTYAEPG------------AD 1406
Cdd:cd22193 58 TDNLKRFINAEYTDEYYEgqTALHIAIERRQGDIVALLVENGADVHAHAK----GRFFQPKYQGEGfyfgelplslaaCT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1407 ASFEIEDFLLK---KGANVNKRDNHGRVPLHYAFLKTGNQNTPIDPIETVSSLCAVR------DLEIDVADNHKR-TPLH 1476
Cdd:cd22193 134 NQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVADNTKENTKFVTRMYDMILIRgaklcpTVELEEIRNNDGlTPLQ 213
|
....*.
gi 470409102 1477 YAAQRG 1482
Cdd:cd22193 214 LAAKMG 219
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1337-1451 |
4.24e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.13 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1337 LAIINSLLRAKANVNIQDSQHKTPLHYALQ-----RKNMNLVRILVQAGADVNASDNNGSSGLHYAVTyaePGADASFEI 1411
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLS---NGYINNLEI 127
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 470409102 1412 EDFLLKKGANVNKRDNHGRVPLHyAFLKTGNqNTPIDPIE 1451
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQ-VYLQSNH-HIDIEIIK 165
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
864-1082 |
4.63e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.96 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 864 LELLVENGADPNAPNDWKTTPLAIALQKGHlacadflleqpsvdvNIRDDdgrtlasqlMDIVCesshkqlqyLIEKKSA 943
Cdd:PHA03100 51 VKILLDNGADINSSTKNNSTPLHYLSNIKY---------------NLTDV---------KEIVK---------LLLEYGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 944 DVTTPDTKGLTPLHYVA----QNFDPVQAAAEFKADNDNSDADSTSP---SVNAGKDDMDvdgkdkgkekgdddkeevge 1016
Cdd:PHA03100 98 NVNAPDNNGITPLLYAIskksNSYSIVEYLLDNGANVNIKNSDGENLlhlYLESNKIDLK-------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1017 ndepkkkkkktwtnwsvvIAKMLIKHGADVNAQT--------------KDK--STPLMLAKTRDNEELLILLLDNGAQIA 1080
Cdd:PHA03100 158 ------------------ILKLLIDKGVDINAKNrvnyllsygvpiniKDVygFTPLHYAVYNNNPEFVKYLLDLGANPN 219
|
..
gi 470409102 1081 AI 1082
Cdd:PHA03100 220 LV 221
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
1852-1928 |
4.97e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.96 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1852 GIDPNVQDEQGKTALHhVVSPLDygsyeNVALLTMLLKAGADPNVKDNQGHTPLYYaLQQRDGVMAARLRSL---GAKLD 1928
Cdd:PHA02946 62 GYSPNETDDDGNYPLH-IASKIN-----NNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIERINLLvqyGAKIN 134
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
781-810 |
5.34e-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: 36.41 E-value: 5.34e-03
10 20 30
....*....|....*....|....*....|
gi 470409102 781 NRMTPLHHAVALGFVDVAKELVEAGCNIEA 810
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
1035-1112 |
5.52e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 5.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 470409102 1035 IAKMLIKHGADVNAQTKDK-STPLMLAKTRDNEELLILLLDNGAQIAAIHVQDRNVLHQLTPQLMErdllPLLEAIARN 1112
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNK----PIVHILLEN 223
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1852-1909 |
6.08e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.16 E-value: 6.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 1852 GIDPNVQDEQGKTALHHVVSpldyGSYENVALLtmLLKAGADPNVKDNQGHTPLYYAL 1909
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAAS----KGYEDCVLV--LLKHACNVHIRDANGNTALWNAI 599
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
882-938 |
6.21e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.87 E-value: 6.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 470409102 882 TTPLAIALQKGHLACADFLLEQPsVDVNIRDDDGRTlasqLMDIVCESSHKQ-LQYLI 938
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKG-ADINAVDGNGET----ALHFAASNGNVEvLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1365-1444 |
7.07e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.74 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1365 LQRKNMNL--VRILVQAGADVNASDNNGSSGLHYAVTYAEPgADASFEIEDFLLKKGANVNKRDNHGRVPLhYAFLKTGN 1442
Cdd:PHA02798 44 LQRDSPSTdiVKLFINLGANVNGLDNEYSTPLCTILSNIKD-YKHMLDIVKILIENGADINKKNSDGETPL-YCLLSNGY 121
|
..
gi 470409102 1443 QN 1444
Cdd:PHA02798 122 IN 123
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
1252-1352 |
8.68e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.36 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1252 NAQDRK--METPLHLAINGDR--QDVFNMLLaeSSINANVADSLGTLPLHLAVNRQNLAMVDALLQANTDVDKWQR-GRA 1326
Cdd:PHA02798 216 NKSHKKkfMEYLNSLLYDNKRfkKNILDFIF--SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITElGNT 293
|
90 100
....*....|....*....|....*.
gi 470409102 1327 ALHTAVDCCNLAIINSLLRAKANVNI 1352
Cdd:PHA02798 294 CLFTAFENESKFIFNSILNKKPNKNT 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
1648-1916 |
9.02e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.10 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1648 ERGVAMNVIDKHGRLPLHYASKNGCGVLVDFFLKrSKSDVNLIDENGKSPLVYAVlgshlqvaerlmarkadcsaldarv 1727
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAI------------------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1728 kqknqahgRHNTPEkkqrrhakaaaaLSKVAQEThlviyamrasladllnlllanKADLNAKDSLGNTCLIYAVRNNDTD 1807
Cdd:PHA02874 166 --------KHNFFD------------IIKLLLEK---------------------GAYANVKDNNGESPLHNAAEYGDYA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470409102 1808 MVHLLFTkrRGAAKPGPSSSSSSSSAPPSSLSPAEPELMLENETgidPNVQDEQGKTALHHVVSPLDygsyeNVALLTML 1887
Cdd:PHA02874 205 CIKLLID--HGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS---INDQDIDGSTPLHHAINPPC-----DIDIIDIL 274
|
250 260 270
....*....|....*....|....*....|.
gi 470409102 1888 LKAGADPNVKDNQGHTPLYYALQ--QRDGVM 1916
Cdd:PHA02874 275 LYHKADISIKDNKGENPIDTAFKyiNKDPVI 305
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| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1861-1899 |
9.81e-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: 9.81e-03
10 20 30
....*....|....*....|....*....|....*....
gi 470409102 1861 QGKTALHHVVspldyGSYENVALLTMLLKAGADPNVKDN 1899
Cdd:pfam00023 1 DGNTPLHLAA-----GRRGNLEIVKLLLSKGADVNARDK 34
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