|
Name |
Accession |
Description |
Interval |
E-value |
| parp_like |
cd01437 |
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
1872-2238 |
5.27e-110 |
|
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: 354.65 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1872 KNTEKDPIRRMIADISDAKTLKTYASQVQmYGGSSQPFGRFTKENIEKAKLVLDKLEKNANRIKQMveaqtgvvesnlld 1951
Cdd:cd01437 1 KSKLDKPVQELIKLIFDVEMMKKAMTELK-IDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQ-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1952 aYITTSELSGDYYSLIPsGEYEFSNLTRLDNVEEIARHRARLNRCQEIETATRLLCAAE-FRQDLDRVDYIrsAIQCEYR 2030
Cdd:cd01437 66 -GSQLEELSNEFYTLIP-HDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEdDSDDPLDANYE--KLKCKIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2031 LETPDSDISQRLLQWIHNSGGK----QAKVKMILEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPS 2106
Cdd:cd01437 142 PLDKDSEEYKIIEKYLKNTHAPtteyTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2107 ACKNGNLFGSGIYLADSFEKSTHYCQPSAG-GINYMLVCQTALGKVRTLDTIPYHYMNqssssAEKYEDTLHYIGDRFPA 2185
Cdd:cd01437 222 APVTGYMFGKGIYFADMFSKSANYCHASASdPTGLLLLCEVALGKMNELKKADYMAKE-----LPKGKHSVKGLGKTAPD 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 2186 GSLT---NDGVGMPLLPLRKRDPIQGSnygfgTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:cd01437 297 PSEFeidLDGVVVPLGKPVPSGHKTDT-----SLLYNEYIVYDVAQVRLKYLLEVK 347
|
|
| PLN03124 |
PLN03124 |
poly [ADP-ribose] polymerase; Provisional |
1762-2238 |
5.91e-45 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 174.64 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLmygrcGFHN--FYRMQIIKRRDAELFILFTNWGRIGSGMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWA 1839
Cdd:PLN03124 177 YDAMLNQTNV-----GDNNnkFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1840 PLANFRDMPKKYRLVETDSTPTSLA--EIELTWK----KNTEKDP-IRRMIADISDAKTLKtyasQVQM---YGGSSQPF 1909
Cdd:PLN03124 252 DRKNFISHPKKYTWLEMDYEDEEESkkDKPSVSSedknKQSKLDPrVAQFISLICDVSMMK----QQMMeigYNARKLPL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1910 GRFTKENIEKAKLVLDKLeknanrikqmveaqtgvveSNLLDAYITTS--ELSGDYYSLIPSgEYEFSNLTR--LDNVEE 1985
Cdd:PLN03124 328 GKLSKSTILKGYEVLKRI-------------------AEVISRSDRETleELSGEFYTVIPH-DFGFKKMRQftIDTPQK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1986 IARHRARLNRCQEIETATRLLCAAEFRQDlDRVDYIRSAIQCEYR-LETpDSDISQRLLQWIHNSGGK-----QAKVKMI 2059
Cdd:PLN03124 388 LKHKLEMVEALGEIEIATKLLKDDIGEQD-DPLYAHYKRLNCELEpLDT-DSEEFSMIAKYLENTHGQthsgyTLEIVQI 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2060 LEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYCQPSAGG-I 2138
Cdd:PLN03124 466 FKVSREGEDERFQKFSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANpD 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2139 NYMLVCQTALGKVRTLDTIPYHymnqssssaekyedtlhyiGDRFPAGSLTNDGVG--MP------------LLPLRKrd 2204
Cdd:PLN03124 546 GVLLLCEVALGDMNELLQADYN-------------------ANKLPPGKLSTKGVGrtVPdpseaktledgvVVPLGK-- 604
|
490 500 510
....*....|....*....|....*....|....
gi 72001594 2205 PIQgSNYGFGTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:PLN03124 605 PVE-SPYSKGSLEYNEYIVYNVDQIRMRYVLQVK 637
|
|
| WGR_PARP |
cd07997 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
1755-1858 |
2.44e-36 |
|
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: 133.58 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1755 CDETQQYFDVLMNKTDLMYGRcgfHNFYRMQIIKRRDAELFILFTNWGRIGsGMGEFQTTPFNSLELAAKEFKSIFKSKS 1834
Cdd:cd07997 3 YGDIATVYDATLNQTDISNNN---NKFYKIQILESKGPNTYALFTRWGRVG-ERGQSQLTPFGSLESAIKEFEKKFKDKT 78
|
90 100
....*....|....*....|....
gi 72001594 1835 GNEWAPLANFRDMPKKYRLVETDS 1858
Cdd:cd07997 79 GNEWENRPLFKKQPGKYALVELDY 102
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
327-635 |
2.21e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.78 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 327 KLPAKILPVSVAKKAYMNKNITPLHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLLKNGGSVT 406
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 407 MLTKQTETPLHVAARAGRAVnctflMKEMLdLEKGDDgestiradrsiINARTRSGNSALHLAVLRNNLDVVDALLAEPT 486
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLE-----IVKLL-LEAGAD-----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 487 ivvdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGN 566
Cdd:COG0666 145 ----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 567 TAAHYAAAYGFLDCLKLLASIDDNILsEPNDWQLYPLSVAYLKGHYGIVTWLLEGPHKDKANINAKDNN 635
Cdd:COG0666 221 TALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PARP |
pfam00644 |
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
2055-2238 |
1.92e-32 |
|
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: 125.91 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2055 KVKMILEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYCQPS 2134
Cdd:pfam00644 24 FILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTGYMFGKGIYFADDASKSANYCPPS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2135 -AGGINYMLVCQTALGKVRTLDTIPYhymnqsSSSAEKYEDTLHYIGDRFPAGSLTNDGVgmpllPLRKrdpIQGSNYGF 2213
Cdd:pfam00644 104 eAHGNGLMLLSEVALGDMNELKKADY------AEKLPPGKHSVKGLGKTAPESFVDLDGV-----PLGK---LVATGYDS 169
|
170 180
....*....|....*....|....*
gi 72001594 2214 GTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:pfam00644 170 SVLLYNEYVVYNVNQVRPKYLLEVK 194
|
|
| WGR |
smart00773 |
Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
1757-1845 |
1.13e-22 |
|
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: 93.89 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1757 ETQQYFDVLMNKTDLMYGRcgfHNFYRMQIIKRRDAElFILFTNWGRIGSGmGEFQTTPFNSLELAAKEFKSIFKSKSGN 1836
Cdd:smart00773 1 EGGEIYDVYLNFTDLASNN---NKFYIIQLLEDDFGG-YSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKN 75
|
....*....
gi 72001594 1837 EWAPLANFR 1845
Cdd:smart00773 76 GYEERGKFV 84
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
512-810 |
4.09e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 96.18 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 512 LEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLLASIDDNI 591
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 592 LsEPNDWQLYPLSVAYLKGHYGIVTWLLEgphkDKANINAKDNNGATLLSnllsYADETMHKELlsqIEYLVARKADASL 671
Cdd:COG0666 81 N-AKDDGGNTLLHAAARNGDLEIVKLLLE----AGADVNARDKDGETPLH----LAAYNGNLEI---VKLLLEAGADVNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLfsmqriilkgsgeAAENdamrmtldNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNGNLMLFNLMLD 751
Cdd:COG0666 149 QDNDGNTPLHL-------------AAAN--------GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72001594 752 KVA--NKRNLFEKWANH---QNFLHEILALPMKVYGDQVLWKGETLTKPAYDVLPILKELHENL 810
Cdd:COG0666 208 AGAdvNAKDNDGKTALDlaaENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| WGR |
pfam05406 |
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
1762-1845 |
9.73e-20 |
|
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: 85.37 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLMYGRcgfHNFYRMQIiKRRDAELFILFTNWGRIGSgMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWAPL 1841
Cdd:pfam05406 1 YDLYLEQTDAARNS---NKFYEIQV-EDDLFGGYSLFRRWGRIGT-RGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRER 75
|
....
gi 72001594 1842 ANFR 1845
Cdd:pfam05406 76 GEFE 79
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
448-752 |
6.72e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.23 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 448 IRADRSIINARTRSGNSALHLAVLRNN---LDVVDALLaEPTIVVDNPTSTGqnrLTPLMM-ACGKGYLEMAKKLVEKGA 523
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLL-EAGADVNAPERCG---FTPLHLyLYNATTLDVIKLLIKAGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 524 LVEGKDKKKRTPLiHAMLNGQ-IH--TAAFLLAKGASLTLADSSGNTAAHYaaaygfldclkLLASIDDNIlsepndwql 600
Cdd:PHA03095 109 DVNAKDKVGRTPL-HVYLSGFnINpkVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANV--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 601 yplsvaylkghyGIVTWLLEGphkdKANINAKDNNGATLLSNLLSYAdetmhKELLSQIEYLVARKADASLADSSGQTPL 680
Cdd:PHA03095 168 ------------ELLRLLIDA----GADVYAVDDRFRSLLHHHLQSF-----KPRARIVRELIRAGCDPAATDMLGNTPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 681 HLFSMQR---------IILKGSGEAAENDAMRMTLdNYKKCFNT------LIKAGAKVDVYDHEDNTPLHYALTNGNLML 745
Cdd:PHA03095 227 HSMATGSsckrslvlpLLIAGISINARNRYGQTPL-HYAAVFNNpracrrLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
|
....*..
gi 72001594 746 FNLMLDK 752
Cdd:PHA03095 306 VRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
466-562 |
4.23e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 466 LHLAVLRNNLDVVDALLAEPTivvdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALveGKDKKKRTPLIHAMLNGQI 545
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA----DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 72001594 546 HTAAFLLAKGASLTLAD 562
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1017-1196 |
5.14e-14 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 74.99 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1017 HYAARVNSHKTVGLFKMIESKGVRRETNDDGRSVLHVAtlACDGSADSVLepiAWLSTRCPIDAVDKFNRTALHYAFGNE 1096
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA--ARNGDLEIVK---LLLEAGADVNARDKDGETPLHLAAYNG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1097 NdfkegnvpfgesdpIAVVSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVH 1176
Cdd:COG0666 132 N--------------LEIVKLL--LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
|
170 180
....*....|....*....|
gi 72001594 1177 HGRQSSALTLIQANADVTEK 1196
Cdd:COG0666 196 NGHLEIVKLLLEAGADVNAK 215
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
512-762 |
9.31e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 512 LEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKllASIDDNI 591
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK--AIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 592 LSEPNDwqlypLSVAYLKGHYGIVTWLLEgpHKDKANINAKDNNGATLLSnllsYADETmhKELLSQIEYLVARKADASL 671
Cdd:PHA02876 236 NINKND-----LSLLKAIRNEDLETSLLL--YDAGFSVNSIDDCKNTPLH----HASQA--PSLSRLVPKLLERGADVNA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLFS--------MQRIILKGsgeAAENDAMRM---------TLDNYKKCFNTLIKAGAKVDVYDHEDNTPL 734
Cdd:PHA02876 303 KNIKGETPLYLMAkngydtenIRTLIMLG---ADVNAADRLyitplhqasTLDRNKDIVITLLELGANVNARDYCDKTPI 379
|
250 260
....*....|....*....|....*...
gi 72001594 735 HYALTNGNLMLFNLMLDKVANKRNLFEK 762
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQK 407
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1112-1196 |
3.21e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.81 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1112 IAVVSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIrKKCHVDLKNkDGNTPLALAVHHGRQSSALTLIQANA 1191
Cdd:pfam12796 10 LELVKLL--LENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGA 85
|
....*
gi 72001594 1192 DVTEK 1196
Cdd:pfam12796 86 DINVK 90
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1027-1178 |
9.91e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1027 TVGLFKMIESKGVRRETNDD-GRSVLHVATLACDGSADSVLEPIAwlsTRCPIDAVDKFNRTALHYAfgnendfkegnvp 1105
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDrFRSLLHHHLQSFKPRARIVRELIR---AGCDPAATDMLGNTPLHSM------------- 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72001594 1106 fgesdpIAVVSLLSSLIRPEQIEIADVN-----GNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVHHG 1178
Cdd:PHA03095 230 ------ATGSSCKRSLVLPLLIAGISINarnryGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
412-570 |
3.22e-05 |
|
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: 49.24 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 412 TETPLHVAARAgravNCTFLMKEMLdlekgddgestiRADRSIINARTRSGNSALHLAVLRNNLDVVDALLAEPTIVVDN 491
Cdd:cd22192 17 SESPLLLAAKE----NDVQAIKKLL------------KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 492 P-TSTGQNRLTPLMMACGKGYLEMAKKLVEKGALV-----------EGKDKK---KRTPLIHAMLNGQIHTAAFLLAKGA 556
Cdd:cd22192 81 PmTSDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffrPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
|
170
....*....|....
gi 72001594 557 SLTLADSSGNTAAH 570
Cdd:cd22192 161 DIRAQDSLGNTVLH 174
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1387-1488 |
3.38e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 48.03 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1387 LLIYMNEKSVSSEAIGFLEELRQMRGVNIDALCQLEIPGKFKKILDYGLIPPISFAVLQENPNMIRALRNAGASLKTQDD 1466
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100
....*....|....*....|..
gi 72001594 1467 YGRTPLMYAIMTNNRSVVDAIV 1488
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLL 140
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1439-1488 |
1.18e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.80 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 72001594 1439 ISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVVDAIV 1488
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
659-756 |
4.37e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.25 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 659 IEYLVARKADASLADSSGQTPLHLfsmqriilkgsgeAAENdamrmtldNYKKCFNTLIKaGAKVDVYDHeDNTPLHYAL 738
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHL-------------AAKN--------GHLEIVKLLLE-HADVNLKDN-GRTALHYAA 69
|
90
....*....|....*...
gi 72001594 739 TNGNLMLFNLMLDKVANK 756
Cdd:pfam12796 70 RSGHLEIVKLLLEKGADI 87
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
456-570 |
3.84e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.38 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 456 NARTRSGNSALHLAVLrNNLDVVDALLA----------EPTIVVDNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALV 525
Cdd:TIGR00870 76 SCRGAVGDTLLHAISL-EYVDAVEAILLhllaafrksgPLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASV 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 526 EGK------DKKKRTPLIH---AMLN-----GQIHTAAFLLAKGASLTLADSSGNTAAH 570
Cdd:TIGR00870 155 PARacgdffVKSQGVDSFYhgeSPLNaaaclGSPSIVALLSEDPADILTADSLGNTLLH 213
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
602-767 |
5.09e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 41.99 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 602 PLSVAYLKGHYGIVTWLLEgphkDKANINAKDNNGATLLSnllSYADETMHKEL----------LSQIEYLVARKADASL 671
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLE----RGASVPARACGDFFVKS---QGVDSFYHGESplnaaaclgsPSIVALLSEDPADILT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLFSMQriilkgSGEAAENDAMRMTldnykkCFNTLIKAGAKVD-------VYDHEDNTPLHYALTNGNLM 744
Cdd:TIGR00870 204 ADSLGNTLLHLLVME------NEFKAEYEELSCQ------MYNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIV 271
|
170 180
....*....|....*....|...
gi 72001594 745 LFNLMLDKVANKRNlFEKWANHQ 767
Cdd:TIGR00870 272 LFRLKLAIKYKQKK-FVAWPNGQ 293
|
|
| WGR |
COG3831 |
WGR domain, predicted DNA-binding domain in MolR [Transcription]; |
1781-1833 |
7.19e-03 |
|
WGR domain, predicted DNA-binding domain in MolR [Transcription];
Pssm-ID: 443043 Cd Length: 83 Bit Score: 37.66 E-value: 7.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 1781 FYRMQIikrrDAELF---ILFTNWGRIGSgMGEFQTTPFNSLELAAKEFKSIFKSK 1833
Cdd:COG3831 17 FYELEV----EPDLFggwSLTRRWGRIGT-KGQTKTKTFASEEEALAALEKLVAEK 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| parp_like |
cd01437 |
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
1872-2238 |
5.27e-110 |
|
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: 354.65 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1872 KNTEKDPIRRMIADISDAKTLKTYASQVQmYGGSSQPFGRFTKENIEKAKLVLDKLEKNANRIKQMveaqtgvvesnlld 1951
Cdd:cd01437 1 KSKLDKPVQELIKLIFDVEMMKKAMTELK-IDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQ-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1952 aYITTSELSGDYYSLIPsGEYEFSNLTRLDNVEEIARHRARLNRCQEIETATRLLCAAE-FRQDLDRVDYIrsAIQCEYR 2030
Cdd:cd01437 66 -GSQLEELSNEFYTLIP-HDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEdDSDDPLDANYE--KLKCKIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2031 LETPDSDISQRLLQWIHNSGGK----QAKVKMILEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPS 2106
Cdd:cd01437 142 PLDKDSEEYKIIEKYLKNTHAPtteyTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2107 ACKNGNLFGSGIYLADSFEKSTHYCQPSAG-GINYMLVCQTALGKVRTLDTIPYHYMNqssssAEKYEDTLHYIGDRFPA 2185
Cdd:cd01437 222 APVTGYMFGKGIYFADMFSKSANYCHASASdPTGLLLLCEVALGKMNELKKADYMAKE-----LPKGKHSVKGLGKTAPD 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 2186 GSLT---NDGVGMPLLPLRKRDPIQGSnygfgTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:cd01437 297 PSEFeidLDGVVVPLGKPVPSGHKTDT-----SLLYNEYIVYDVAQVRLKYLLEVK 347
|
|
| PLN03124 |
PLN03124 |
poly [ADP-ribose] polymerase; Provisional |
1762-2238 |
5.91e-45 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 174.64 E-value: 5.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLmygrcGFHN--FYRMQIIKRRDAELFILFTNWGRIGSGMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWA 1839
Cdd:PLN03124 177 YDAMLNQTNV-----GDNNnkFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1840 PLANFRDMPKKYRLVETDSTPTSLA--EIELTWK----KNTEKDP-IRRMIADISDAKTLKtyasQVQM---YGGSSQPF 1909
Cdd:PLN03124 252 DRKNFISHPKKYTWLEMDYEDEEESkkDKPSVSSedknKQSKLDPrVAQFISLICDVSMMK----QQMMeigYNARKLPL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1910 GRFTKENIEKAKLVLDKLeknanrikqmveaqtgvveSNLLDAYITTS--ELSGDYYSLIPSgEYEFSNLTR--LDNVEE 1985
Cdd:PLN03124 328 GKLSKSTILKGYEVLKRI-------------------AEVISRSDRETleELSGEFYTVIPH-DFGFKKMRQftIDTPQK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1986 IARHRARLNRCQEIETATRLLCAAEFRQDlDRVDYIRSAIQCEYR-LETpDSDISQRLLQWIHNSGGK-----QAKVKMI 2059
Cdd:PLN03124 388 LKHKLEMVEALGEIEIATKLLKDDIGEQD-DPLYAHYKRLNCELEpLDT-DSEEFSMIAKYLENTHGQthsgyTLEIVQI 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2060 LEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYCQPSAGG-I 2138
Cdd:PLN03124 466 FKVSREGEDERFQKFSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANpD 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2139 NYMLVCQTALGKVRTLDTIPYHymnqssssaekyedtlhyiGDRFPAGSLTNDGVG--MP------------LLPLRKrd 2204
Cdd:PLN03124 546 GVLLLCEVALGDMNELLQADYN-------------------ANKLPPGKLSTKGVGrtVPdpseaktledgvVVPLGK-- 604
|
490 500 510
....*....|....*....|....*....|....
gi 72001594 2205 PIQgSNYGFGTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:PLN03124 605 PVE-SPYSKGSLEYNEYIVYNVDQIRMRYVLQVK 637
|
|
| WGR_PARP |
cd07997 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
1755-1858 |
2.44e-36 |
|
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: 133.58 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1755 CDETQQYFDVLMNKTDLMYGRcgfHNFYRMQIIKRRDAELFILFTNWGRIGsGMGEFQTTPFNSLELAAKEFKSIFKSKS 1834
Cdd:cd07997 3 YGDIATVYDATLNQTDISNNN---NKFYKIQILESKGPNTYALFTRWGRVG-ERGQSQLTPFGSLESAIKEFEKKFKDKT 78
|
90 100
....*....|....*....|....
gi 72001594 1835 GNEWAPLANFRDMPKKYRLVETDS 1858
Cdd:cd07997 79 GNEWENRPLFKKQPGKYALVELDY 102
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
327-635 |
2.21e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.78 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 327 KLPAKILPVSVAKKAYMNKNITPLHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLLKNGGSVT 406
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 407 MLTKQTETPLHVAARAGRAVnctflMKEMLdLEKGDDgestiradrsiINARTRSGNSALHLAVLRNNLDVVDALLAEPT 486
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLE-----IVKLL-LEAGAD-----------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 487 ivvdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGN 566
Cdd:COG0666 145 ----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 567 TAAHYAAAYGFLDCLKLLASIDDNILsEPNDWQLYPLSVAYLKGHYGIVTWLLEGPHKDKANINAKDNN 635
Cdd:COG0666 221 TALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| PARP |
pfam00644 |
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
2055-2238 |
1.92e-32 |
|
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: 125.91 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2055 KVKMILEISPMLSTEKFEPFVNDDNQKFLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYCQPS 2134
Cdd:pfam00644 24 FILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVTGYMFGKGIYFADDASKSANYCPPS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2135 -AGGINYMLVCQTALGKVRTLDTIPYhymnqsSSSAEKYEDTLHYIGDRFPAGSLTNDGVgmpllPLRKrdpIQGSNYGF 2213
Cdd:pfam00644 104 eAHGNGLMLLSEVALGDMNELKKADY------AEKLPPGKHSVKGLGKTAPESFVDLDGV-----PLGK---LVATGYDS 169
|
170 180
....*....|....*....|....*
gi 72001594 2214 GTLDFSEYIVRNPNRVLPKYIVMYK 2238
Cdd:pfam00644 170 SVLLYNEYVVYNVNQVRPKYLLEVK 194
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
416-691 |
5.30e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.98 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 416 LHVAARAGRAVNCTFLMKEMLDLEKGDDGESTIRADRSIINARTRSGNSALHLAVLRNNLDVVDALLAEPTIVVDNPTST 495
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 496 GQnrlTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAY 575
Cdd:COG0666 87 GN---TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 576 GFLDCLKLL--ASIDDNIlsePNDWQLYPLSVAYLKGHYGIVTWLLEGphkdKANINAKDNNGATllsnLLSYADETMHK 653
Cdd:COG0666 164 GNLEIVKLLleAGADVNA---RDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDGKT----ALDLAAENGNL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 72001594 654 ELlsqIEYLVARKADASLADSSGQTPLHLFSMQRIILK 691
Cdd:COG0666 233 EI---VKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
|
| PLN03123 |
PLN03123 |
poly [ADP-ribose] polymerase; Provisional |
1762-2229 |
4.94e-26 |
|
poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 215590 [Multi-domain] Cd Length: 981 Bit Score: 117.58 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLMYGRcgfHNFYRMQIIKRRDAELFILFTNWGRIGS-GMGEFQTTPFNSLElAAKEFKSIFKSKSGNEWAP 1840
Cdd:PLN03123 520 YNTTLNMSDLSTGV---NSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEMSKSD-AIHEFKRLFLEKTGNPWES 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1841 L---ANFRDMPKKYRLVETDSTPTSLAEIELTWKKNTEKDP----IRRMIADIsdaktlKTYAS-----QVQMyggSSQP 1908
Cdd:PLN03123 596 WeqkTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPrlveLMKMLFDV------ETYRAammefEINM---SEMP 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1909 FGRFTKENIEKAKLVLDKLEKNANRIKQmveaQTGVVESNLLDAyittselSGDYYSLIPS-------GEYEFSNLTRLd 1981
Cdd:PLN03123 667 LGKLSKANIQKGFEALTEIQNLLKENDQ----DPSIRESLLVDA-------SNRFFTLIPSihphiirDEDDLKSKVKM- 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1982 nveeiarhrarLNRCQEIETATRLLCAAEFRQDLDRVDYIRsaIQCEYRLETPDSDISQRLLQWIHNSGGKQAKvKMILE 2061
Cdd:PLN03123 735 -----------LEALQDIEIASRLVGFDVDEDDSLDDKYKK--LHCDISPLPHDSEDYKLIEKYLLTTHAPTHT-DWSLE 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2062 ISPMLSTE------KFEPFVND-DNQKFLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYCQPS 2134
Cdd:PLN03123 801 LEEVFSLEregefdKYAPYKEKlKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTD 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2135 AGG-INYMLVCQTALGKVRTLDTIpyHYMnqssssaekyedtlhyigDRFPAGSLTNDGVG--MPL------------LP 2199
Cdd:PLN03123 881 RKNpVGLMLLSEVALGEIYELKKA--KYM------------------DKPPRGKHSTKGLGktVPQesefvkwrddvvVP 940
|
490 500 510
....*....|....*....|....*....|
gi 72001594 2200 LRKRDPiqgSNYGFGTLDFSEYIVRNPNRV 2229
Cdd:PLN03123 941 CGKPVP---SKVKASELMYNEYIVYNTAQV 967
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
479-758 |
1.70e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 108.89 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 479 DALLAEPTIVVDNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASL 558
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 559 TLADSSGNTAAHYAAAYGFLDCLKLLASIDDNILSePNDWQLYPLSVAYLKGHYGIVTWLLEGphkdKANINAKDNNGAT 638
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA-RDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGNT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 639 llsnLLSYADETMHKELlsqIEYLVARKADASLADSSGQTPLHLfsmqriilkgsgeAAENdamrmtldNYKKCFNTLIK 718
Cdd:COG0666 156 ----PLHLAAANGNLEI---VKLLLEAGADVNARDNDGETPLHL-------------AAEN--------GHLEIVKLLLE 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 72001594 719 AGAKVDVYDHEDNTPLHYALTNGNLMLFNLMLDKVANKRN 758
Cdd:COG0666 208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
261-569 |
2.67e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 105.42 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 261 LIEDNVTYTKLYQLCKIPDGPIVEHHIEMHFVTAVRMGHRDLASALAQGPVKMHCNDLHRATLKDQKLPAKILPVSVAKK 340
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 341 AYMNKNITPLHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLLKNGGSVTMLTKQTETPLHVAA 420
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 421 RAGRAVNCTFLmkemldLEKGDDgestiradrsiINARTRSGNSALHLAVLRNNLDVVDALLAEPtivvDNPTSTGQNRL 500
Cdd:COG0666 162 ANGNLEIVKLL------LEAGAD-----------VNARDNDGETPLHLAAENGHLEIVKLLLEAG----ADVNAKDNDGK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 501 TPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAA 569
Cdd:COG0666 221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| WGR |
smart00773 |
Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
1757-1845 |
1.13e-22 |
|
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: 93.89 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1757 ETQQYFDVLMNKTDLMYGRcgfHNFYRMQIIKRRDAElFILFTNWGRIGSGmGEFQTTPFNSLELAAKEFKSIFKSKSGN 1836
Cdd:smart00773 1 EGGEIYDVYLNFTDLASNN---NKFYIIQLLEDDFGG-YSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKN 75
|
....*....
gi 72001594 1837 EWAPLANFR 1845
Cdd:smart00773 76 GYEERGKFV 84
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
512-810 |
4.09e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 96.18 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 512 LEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLLASIDDNI 591
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 592 LsEPNDWQLYPLSVAYLKGHYGIVTWLLEgphkDKANINAKDNNGATLLSnllsYADETMHKELlsqIEYLVARKADASL 671
Cdd:COG0666 81 N-AKDDGGNTLLHAAARNGDLEIVKLLLE----AGADVNARDKDGETPLH----LAAYNGNLEI---VKLLLEAGADVNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLfsmqriilkgsgeAAENdamrmtldNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNGNLMLFNLMLD 751
Cdd:COG0666 149 QDNDGNTPLHL-------------AAAN--------GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72001594 752 KVA--NKRNLFEKWANH---QNFLHEILALPMKVYGDQVLWKGETLTKPAYDVLPILKELHENL 810
Cdd:COG0666 208 AGAdvNAKDNDGKTALDlaaENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| WGR |
pfam05406 |
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
1762-1845 |
9.73e-20 |
|
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: 85.37 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLMYGRcgfHNFYRMQIiKRRDAELFILFTNWGRIGSgMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWAPL 1841
Cdd:pfam05406 1 YDLYLEQTDAARNS---NKFYEIQV-EDDLFGGYSLFRRWGRIGT-RGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRER 75
|
....
gi 72001594 1842 ANFR 1845
Cdd:pfam05406 76 GEFE 79
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
448-752 |
6.72e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.23 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 448 IRADRSIINARTRSGNSALHLAVLRNN---LDVVDALLaEPTIVVDNPTSTGqnrLTPLMM-ACGKGYLEMAKKLVEKGA 523
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLL-EAGADVNAPERCG---FTPLHLyLYNATTLDVIKLLIKAGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 524 LVEGKDKKKRTPLiHAMLNGQ-IH--TAAFLLAKGASLTLADSSGNTAAHYaaaygfldclkLLASIDDNIlsepndwql 600
Cdd:PHA03095 109 DVNAKDKVGRTPL-HVYLSGFnINpkVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRNANV--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 601 yplsvaylkghyGIVTWLLEGphkdKANINAKDNNGATLLSNLLSYAdetmhKELLSQIEYLVARKADASLADSSGQTPL 680
Cdd:PHA03095 168 ------------ELLRLLIDA----GADVYAVDDRFRSLLHHHLQSF-----KPRARIVRELIRAGCDPAATDMLGNTPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 681 HLFSMQR---------IILKGSGEAAENDAMRMTLdNYKKCFNT------LIKAGAKVDVYDHEDNTPLHYALTNGNLML 745
Cdd:PHA03095 227 HSMATGSsckrslvlpLLIAGISINARNRYGQTPL-HYAAVFNNpracrrLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
|
....*..
gi 72001594 746 FNLMLDK 752
Cdd:PHA03095 306 VRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
466-562 |
4.23e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.46 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 466 LHLAVLRNNLDVVDALLAEPTivvdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALveGKDKKKRTPLIHAMLNGQI 545
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGA----DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 72001594 546 HTAAFLLAKGASLTLAD 562
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
503-591 |
5.67e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.07 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 503 LMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASltLADSSGNTAAHYAAAYGFLDCLK 582
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
....*....
gi 72001594 583 LLASIDDNI 591
Cdd:pfam12796 79 LLLEKGADI 87
|
|
| WGR_PARP1_like |
cd08001 |
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ... |
1776-1858 |
6.20e-15 |
|
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: 72.63 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1776 CGFHNFYRMQIIKRRDAELFILFTNWGRIGSGMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWAPLANFRDMPKKYRLVE 1855
Cdd:cd08001 22 TGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFENRKNFKKKPGKFYPLD 101
|
...
gi 72001594 1856 TDS 1858
Cdd:cd08001 102 IDY 104
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
504-746 |
1.14e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 504 MMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLiHAMLNGQIHTAA----FLLAKGASLTLADSSGNTAAHYAAAYGF-L 578
Cdd:PHA03095 19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPL-HLYLHYSSEKVKdivrLLLEAGADVNAPERCGFTPLHLYLYNATtL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 579 DCLKLLASIDDNILSEpNDWQLYPLSVaYLKG---HYGIVTWLLEgphkDKANINAKDNNGATLLSNLLSYADETMhkEL 655
Cdd:PHA03095 98 DVIKLLIKAGADVNAK-DKVGRTPLHV-YLSGfniNPKVIRLLLR----KGADVNALDLYGMTPLAVLLKSRNANV--EL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 656 LsqiEYLVARKADASLADSSGQTPLHLFS---------MQRIILKGSGEAAEND---AMRMTLDNYKKCFNT----LIKA 719
Cdd:PHA03095 170 L---RLLIDAGADVYAVDDRFRSLLHHHLqsfkprariVRELIRAGCDPAATDMlgnTPLHSMATGSSCKRSlvlpLLIA 246
|
250 260
....*....|....*....|....*..
gi 72001594 720 GAKVDVYDHEDNTPLHYALTNGNLMLF 746
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRAC 273
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1017-1196 |
5.14e-14 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 74.99 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1017 HYAARVNSHKTVGLFKMIESKGVRRETNDDGRSVLHVAtlACDGSADSVLepiAWLSTRCPIDAVDKFNRTALHYAFGNE 1096
Cdd:COG0666 57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA--ARNGDLEIVK---LLLEAGADVNARDKDGETPLHLAAYNG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1097 NdfkegnvpfgesdpIAVVSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVH 1176
Cdd:COG0666 132 N--------------LEIVKLL--LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
|
170 180
....*....|....*....|
gi 72001594 1177 HGRQSSALTLIQANADVTEK 1196
Cdd:COG0666 196 NGHLEIVKLLLEAGADVNAK 215
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
512-762 |
9.31e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.56 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 512 LEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKllASIDDNI 591
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK--AIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 592 LSEPNDwqlypLSVAYLKGHYGIVTWLLEgpHKDKANINAKDNNGATLLSnllsYADETmhKELLSQIEYLVARKADASL 671
Cdd:PHA02876 236 NINKND-----LSLLKAIRNEDLETSLLL--YDAGFSVNSIDDCKNTPLH----HASQA--PSLSRLVPKLLERGADVNA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLFS--------MQRIILKGsgeAAENDAMRM---------TLDNYKKCFNTLIKAGAKVDVYDHEDNTPL 734
Cdd:PHA02876 303 KNIKGETPLYLMAkngydtenIRTLIMLG---ADVNAADRLyitplhqasTLDRNKDIVITLLELGANVNARDYCDKTPI 379
|
250 260
....*....|....*....|....*...
gi 72001594 735 HYALTNGNLMLFNLMLDKVANKRNLFEK 762
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQK 407
|
|
| WGR_PARP3_like |
cd08002 |
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ... |
1755-1857 |
9.31e-12 |
|
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: 63.19 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1755 CDETQQYFDVLMNKTDLmygrcGFHN--FYRMQIIkrRDAELFILFTNWGRIG-SGMGEFQTtPFNSLELAAKEFKSIFK 1831
Cdd:cd08002 2 GAEVDEDYDCMLNQTNI-----GHNNnkFYVIQLL--ESGKEYYVWNRWGRVGeKGQNKLKG-PWDSLEGAIKDFEKKFK 73
|
90 100
....*....|....*....|....*.
gi 72001594 1832 SKSGNEWAPLANFRDMPKKYRLVETD 1857
Cdd:cd08002 74 DKTKNNWEDRENFVPHPGKYTLIEMD 99
|
|
| WGR_PARP2_like |
cd08003 |
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
1762-1857 |
9.77e-12 |
|
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: 63.50 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1762 FDVLMNKTDLmygrcGFHN--FYRMQIIKRRDAELFILFTNWGRIGSgMGEFQTTPFNS-LELAAKEFKSIFKSKSGNEW 1838
Cdd:cd08003 10 YDAMLNQTNI-----QQNNnkYYIIQLLEDDAEKIYSVWFRWGRVGK-KGQSSLVPCGSdLEQAKSLFEKKFLDKTKNEW 83
|
90
....*....|....*....
gi 72001594 1839 APLANFRDMPKKYRLVETD 1857
Cdd:cd08003 84 EDRANFEKVAGKYDLLEMD 102
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
923-1197 |
1.22e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 68.06 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 923 DEFLTQKNEKDDVLIVQAIMFDKPNVVELILDTASEMHLIHGTHNAIKENELEVVVHKTIIMYMIEMRMWELIPKVNASS 1002
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1003 EfwkSKDAKGNSVWHYAARVNSHKTVglfKMIESKGVR-RETNDDGRSVLHVATLACDGSADSVLepiawLSTRCPIDAV 1081
Cdd:COG0666 81 N---AKDDGGNTLLHAAARNGDLEIV---KLLLEAGADvNARDKDGETPLHLAAYNGNLEIVKLL-----LEAGADVNAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1082 DKFNRTALHYAFGNENdfkegnvpfgesdpIAVVSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVD 1161
Cdd:COG0666 150 DNDGNTPLHLAAANGN--------------LEIVKLL--LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
|
250 260 270
....*....|....*....|....*....|....*.
gi 72001594 1162 LKNKDGNTPLALAVHHGRQSSALTLIQANADVTEKI 1197
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
416-529 |
2.75e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 416 LHVAARAGRAVNCTFLMKEMLDlekgddgestiradrsiINARTRSGNSALHLAVLRNNLDVVDALLAEPTIVVDNptst 495
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-----------------ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---- 59
|
90 100 110
....*....|....*....|....*....|....
gi 72001594 496 gqNRLTPLMMACGKGYLEMAKKLVEKGALVEGKD 529
Cdd:pfam12796 60 --NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
501-680 |
9.54e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 501 TPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDC 580
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 581 LKLLASIDDNILSEPNDwQLYPLSVAYLKGHyGIVTWLLegphkDKANINAKDNNGATLLSNLLSYADEtmhkelLSQIE 660
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKN-GFTPLHNAIIHNR-SAIELLI-----NNASINDQDIDGSTPLHHAINPPCD------IDIID 272
|
170 180
....*....|....*....|
gi 72001594 661 YLVARKADASLADSSGQTPL 680
Cdd:PHA02874 273 ILLYHKADISIKDNKGENPI 292
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
466-755 |
8.95e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.06 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 466 LHLAVLRNNLDVVDALLAEPTivvdNPTSTGQNRLTPLMMACGKGY-----LEMAKKLVEKGALVEGKDKKKRTPLIHAM 540
Cdd:PHA03100 39 LYLAKEARNIDVVKILLDNGA----DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 541 LN--GQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGF--LDCLKLLasIDDNIlsepndwqlyplsvaylkghygivt 616
Cdd:PHA03100 115 SKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLL--IDKGV------------------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 617 wllegphkdkaNINAKDNngatllsnllsyadetmhkellsqIEYLVARKADASLADSSGQTPLHLfsmqriilkgsgeA 696
Cdd:PHA03100 168 -----------DINAKNR------------------------VNYLLSYGVPINIKDVYGFTPLHY-------------A 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 697 AENdamrmtldNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNGNLMLFNLMLDKVAN 755
Cdd:PHA03100 200 VYN--------NNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
348-620 |
9.19e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 60.42 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 348 TPLHT---AAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAP-MEFLLKNGGSVTMLTKQTETPLHVAARaG 423
Cdd:PHA03095 49 TPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHVYLS-G 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 424 RAVNctFLMKEMLdLEKGDDgestiradrsiINARTRSGNSALHlAVLRN---NLDVVDALLAeptiVVDNPTSTGQNRL 500
Cdd:PHA03095 128 FNIN--PKVIRLL-LRKGAD-----------VNALDLYGMTPLA-VLLKSrnaNVELLRLLID----AGADVYAVDDRFR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 501 TPL--MMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLiHAMLNGQIHTA---AFLLAKGASLTLADSSGNTAAHYAAAY 575
Cdd:PHA03095 189 SLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPL-HSMATGSSCKRslvLPLLIAGISINARNRYGQTPLHYAAVF 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 72001594 576 G----FLDCLKLLASIddNILSEPNdwqLYPLSVAYLKGHYGIVTWLLE 620
Cdd:PHA03095 268 NnpraCRRLIALGADI--NAVSSDG---NTPLSLMVRNNNGRAVRAALA 311
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
383-482 |
3.02e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 53.20 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 383 MHYAACAPGTAPMEFLLKNGGSVTMLTKQTETPLHVAARAGRavncTFLMKEMLDLEKGDDGEstiradrsiinartrSG 462
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH----LEIVKLLLEHADVNLKD---------------NG 61
|
90 100
....*....|....*....|
gi 72001594 463 NSALHLAVLRNNLDVVDALL 482
Cdd:pfam12796 62 RTALHYAARSGHLEIVKLLL 81
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1112-1196 |
3.21e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.81 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1112 IAVVSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIrKKCHVDLKNkDGNTPLALAVHHGRQSSALTLIQANA 1191
Cdd:pfam12796 10 LELVKLL--LENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGA 85
|
....*
gi 72001594 1192 DVTEK 1196
Cdd:pfam12796 86 DINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
513-681 |
3.80e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.05 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 513 EMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLLasIDDNIL 592
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL--LEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 593 SEPNDWQL-YPLSVAYLKGHYGIVTWLLEgphkDKANINAKDNNGATLLSNLLSYADetmhkellSQIEYLVaRKADASL 671
Cdd:PHA02874 183 ANVKDNNGeSPLHNAAEYGDYACIKLLID----HGNHIMNKCKNGFTPLHNAIIHNR--------SAIELLI-NNASIND 249
|
170
....*....|
gi 72001594 672 ADSSGQTPLH 681
Cdd:PHA02874 250 QDIDGSTPLH 259
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
533-584 |
5.07e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.12 E-value: 5.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 72001594 533 RTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLL 584
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
883-1193 |
1.07e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 55.73 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 883 AAVTLANLAMSIPIECGRHQQNQLALFKILIKLSKEFNKVDEFLTQKNEKDDVLIVQAIMFDKPNVVELILD-----TAS 957
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAagadiNAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 958 EMHLIHGTHNAIKENELEVVvhKTIImymiemrmwELIPKVNAssefwksKDAKGNSVWHYAARVNSHKTVglfKMIESK 1037
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIV--KLLL---------EAGADVNA-------RDKDGETPLHLAAYNGNLEIV---KLLLEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1038 GVRRE-TNDDGRSVLHVAtlACDGSADSV--LepiawLSTRCPIDAVDKFNRTALHYAFGNENdfkegnvpfgesdpIAV 1114
Cdd:COG0666 143 GADVNaQDNDGNTPLHLA--AANGNLEIVklL-----LEAGADVNARDNDGETPLHLAAENGH--------------LEI 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 1115 VSLLssLIRPEQIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVHHGRQSSALTLIQANADV 1193
Cdd:COG0666 202 VKLL--LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ADP_ribosyl |
cd01341 |
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ... |
2082-2131 |
3.16e-07 |
|
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: 51.41 E-value: 3.16e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 72001594 2082 FLWHGTKATNLMSILKNGFLIDPPSACKNGNLFGSGIYLADSFEKSTHYC 2131
Cdd:cd01341 1 FLFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYS 50
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
396-755 |
3.99e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.45 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 396 EFLLKNGGSVTMLTKQTETPLHVAARAGRAVNCTFLMkemldlekgddgesTIRADRSIInarTRSGNSALHLAVLRNNL 475
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL--------------SYGADVNII---ALDDLSVLECAVDSKNI 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 476 DVVDAllaeptiVVDNPTSTGQNRLTpLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQI-HTAAFLLAK 554
Cdd:PHA02876 225 DTIKA-------IIDNRSNINKNDLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLER 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 555 GASLTLADSSGNTAAHYAAAYGF-LDCLKLLASIDDNIlSEPNDWQLYPLSVA-YLKGHYGIVTWLLEGphkdKANINAK 632
Cdd:PHA02876 297 GADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV-NAADRLYITPLHQAsTLDRNKDIVITLLEL----GANVNAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 633 D------------NNGATLLSNLLSYADETmhkELLSQieylvarkadasladsSGQTPLHLfsmqriILKGSgeaaend 700
Cdd:PHA02876 372 DycdktpihyaavRNNVVIINTLLDYGADI---EALSQ----------------KIGTALHF------ALCGT------- 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 701 amrmtldNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNG-NLMLFNLMLDKVAN 755
Cdd:PHA02876 420 -------NPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
395-592 |
7.26e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.23 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 395 MEFLLKNGGSVTMLTKQTETPLHVAARAGRAVNctflMKEMLDLEKGDDgestiradrsiiNARTRSGNSALHLAVLRNN 474
Cdd:PHA02875 51 IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA----VEELLDLGKFAD------------DVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 475 LDVVDALLAEPTivvdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAK 554
Cdd:PHA02875 115 LDIMKLLIARGA----DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 72001594 555 GASLTLADSSGNTAAH-YAAAYGFLDCLKLLAS--IDDNIL 592
Cdd:PHA02875 191 GANIDYFGKNGCVAALcYAIENNKIDIVRLFIKrgADCNIM 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
1027-1178 |
9.91e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1027 TVGLFKMIESKGVRRETNDD-GRSVLHVATLACDGSADSVLEPIAwlsTRCPIDAVDKFNRTALHYAfgnendfkegnvp 1105
Cdd:PHA03095 166 NVELLRLLIDAGADVYAVDDrFRSLLHHHLQSFKPRARIVRELIR---AGCDPAATDMLGNTPLHSM------------- 229
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72001594 1106 fgesdpIAVVSLLSSLIRPEQIEIADVN-----GNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVHHG 1178
Cdd:PHA03095 230 ------ATGSSCKRSLVLPLLIAGISINarnryGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
|
|
| PLN03122 |
PLN03122 |
Poly [ADP-ribose] polymerase; Provisional |
1784-2238 |
1.09e-06 |
|
Poly [ADP-ribose] polymerase; Provisional
Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 54.03 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1784 MQIIKRRDAELFILFTNwGRIGSG-MGEFQTTPFNSLELAAKEFKSIFKSKSGNEWAPL---ANFRDMPKKYRLVETDST 1859
Cdd:PLN03122 355 MQLITVPDSNLHLYYKK-GRVGDDpNAEERLEEWEDVDAAIKEFVRLFEEITGNEFEPWereKKFEKKRLKFYPIDMDDG 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1860 ----PTSLAEIEL-TWKKNTEKDPIRRMIADISDAKTLKTYASQVQMYGGSSQPFGRFTKENIEKAKLVLdkleknanri 1934
Cdd:PLN03122 434 vdvrAGGLGLRQLgVAAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVL---------- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1935 KQMVEAQTGVVESNLlDAYITTSELSGDYYSLIPSgeyefSNLTRLDNVEEIARHRAR-LNRCQEIETATRLLcaAEFRQ 2013
Cdd:PLN03122 504 LEFAEFVKSEKETGQ-KAEAMWLDFSNKWFSLVHS-----TRPFVIRDIDELADHAASaLETVRDINVASRLI--GDMTG 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2014 DL------DRVDYIRSAIQCEYRlETPDSDISQRLLQWIHnsggkqAKVKmILEISPMLSTEK-----------FEPFVN 2076
Cdd:PLN03122 576 STlddplsDRYKKLGCSISPVDK-ESDDYKMIVKYLEKTY------EPVK-VGDVSYSVSVENifavessagpsLDEIKK 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2077 DDNQKFLWHGTKATNLMSILKNGFlidPPSACK---NGNLFGSGIYLADSFEKSTHYC-----QPSAgginYMLVCQTAL 2148
Cdd:PLN03122 648 LPNKVLLWCGTRSSNLLRHLAKGF---LPAVCSlpvPGYMFGKAIVCSDAAAEAARYGftavdRPEG----FLVLAVASL 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 2149 GK-VRTLDTIPyhymnQSSSSAEKYEDTLHYIGDRFPAGS---LTNDGVGMP---LLPLRKRDpiqgsnygfGTLDFSEY 2221
Cdd:PLN03122 721 GDeVLELTKPP-----EDVKSYEEKKVGVKGLGRKKTDESehfKWRDDITVPcgrLIPSEHKD---------SPLEYNEY 786
|
490
....*....|....*..
gi 72001594 2222 IVRNPNRVLPKYIVMYK 2238
Cdd:PLN03122 787 AVYDPKQVSIRFLVGVK 803
|
|
| PARP_reg |
pfam02877 |
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ... |
1908-2020 |
6.00e-06 |
|
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: 47.90 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1908 PFGRFTKENIEKAKLVLdkleknaNRIKQMVEAQTGVVESNLLdayittSELSGDYYSLIPSgEYEFSNLTRLDNVEEIA 1987
Cdd:pfam02877 35 PLGKLSKRQIKKGYEVL-------KELSELLKKPSLAKAKAKL------EDLSNRFYTLIPH-DFGRNRPPVIDTEEELK 100
|
90 100 110
....*....|....*....|....*....|...
gi 72001594 1988 RHRARLNRCQEIETATRLLCAAEFRQDLDRVDY 2020
Cdd:pfam02877 101 EKLELLEALLDIEVASKLLKDSKSDDDEHPLDR 133
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
499-552 |
6.57e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 6.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 72001594 499 RLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLL 552
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
469-671 |
9.83e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.37 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 469 AVLRNNLDVVDALLAeptiVVDNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTA 548
Cdd:PHA02875 9 AILFGELDIARRLLD----IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 549 AFLLAKGaslTLAD----SSGNTAAHYAAAYGFLDCLKLLAS--IDDNIlsePNDWQLYPLSVAYLKGHYGIVTWLLegp 622
Cdd:PHA02875 85 EELLDLG---KFADdvfyKDGMTPLHLATILKKLDIMKLLIArgADPDI---PNTDKFSPLHLAVMMGDIKGIELLI--- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 72001594 623 hKDKANINAKDNNGATLLSNLLSYADETMHKELL---SQIEYlVARKADASL 671
Cdd:PHA02875 156 -DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLdsgANIDY-FGKNGCVAA 205
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
396-591 |
1.23e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.05 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 396 EFLLKNGGSVTMLTKQTETPLHvaaragravnctFLMKEMLDLEKGDDGESTIRADRSIINARTRSGNSALHLAVLR--N 473
Cdd:PHA03100 52 KILLDNGADINSSTKNNSTPLH------------YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 474 NLDVVDALLAEpTIVVDNPTSTGQNRLtPLMMACGKGYLEMAKKLVEKGALVEGKDKKKR----------------TPLI 537
Cdd:PHA03100 120 SYSIVEYLLDN-GANVNIKNSDGENLL-HLYLESNKIDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLH 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 72001594 538 HAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLLASIDDNI 591
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
342-526 |
1.84e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.66 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 342 YMNKNITPLH--TAAISNSTHMLEAMRAVY---PTINIPDQDNWYTMHYAACAP-GTAPM-EFLLKNGGSVTMLTKQTET 414
Cdd:PHA03100 64 STKNNSTPLHylSNIKYNLTDVKEIVKLLLeygANVNAPDNNGITPLLYAISKKsNSYSIvEYLLDNGANVNIKNSDGEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 415 PLHVAARagraVNCTFL-MKEMLdLEKGDDGESTIRADRSI-----INARTRSGNSALHLAVLRNNLDVVDALLAEPTiv 488
Cdd:PHA03100 144 LLHLYLE----SNKIDLkILKLL-IDKGVDINAKNRVNYLLsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-- 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 72001594 489 vdNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVE 526
Cdd:PHA03100 217 --NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
344-519 |
2.82e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 344 NKNITPLHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLLKNGGSVTMLTKQTETPLHVAarAG 423
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 424 RAVNCTFLmkEMLdLEKGDD--GESTIRadrsiinartrsGNSALHLAVlrNNLDVVDALLAEPTivvdNPTSTGQNRLT 501
Cdd:PHA02878 244 YCKDYDIL--KLL-LEHGVDvnAKSYIL------------GLTALHSSI--KSERKLKLLLEYGA----DINSLNSYKLT 302
|
170
....*....|....*....
gi 72001594 502 PLMMACGKGY-LEMAKKLV 519
Cdd:PHA02878 303 PLSSAVKQYLcINIGRILI 321
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
412-570 |
3.22e-05 |
|
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: 49.24 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 412 TETPLHVAARAgravNCTFLMKEMLdlekgddgestiRADRSIINARTRSGNSALHLAVLRNNLDVVDALLAEPTIVVDN 491
Cdd:cd22192 17 SESPLLLAAKE----NDVQAIKKLL------------KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 492 P-TSTGQNRLTPLMMACGKGYLEMAKKLVEKGALV-----------EGKDKK---KRTPLIHAMLNGQIHTAAFLLAKGA 556
Cdd:cd22192 81 PmTSDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffrPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
|
170
....*....|....
gi 72001594 557 SLTLADSSGNTAAH 570
Cdd:cd22192 161 DIRAQDSLGNTVLH 174
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1387-1488 |
3.38e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 48.03 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1387 LLIYMNEKSVSSEAIGFLEELRQMRGVNIDALCQLEIPGKFKKILDYGLIPPISFAVLQENPNMIRALRNAGASLKTQDD 1466
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100
....*....|....*....|..
gi 72001594 1467 YGRTPLMYAIMTNNRSVVDAIV 1488
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLL 140
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
624-774 |
3.45e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.87 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 624 KDKANINAKDNNGATLLSNLLSYAdetmHKELLSQIEYLVARKADASLADSSGQTPLHLFS--------MQRIILKGSGE 695
Cdd:PHA03095 35 AAGADVNFRGEYGKTPLHLYLHYS----SEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLynattldvIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 696 AAENDAMRMTLDNYKKCFNT-------LIKAGAKVDVYDHEDNTPLHYAL--TNGNLMLFNLMLDKVAnkrNLFEKWANH 766
Cdd:PHA03095 111 NAKDKVGRTPLHVYLSGFNInpkvirlLLRKGADVNALDLYGMTPLAVLLksRNANVELLRLLIDAGA---DVYAVDDRF 187
|
....*...
gi 72001594 767 QNFLHEIL 774
Cdd:PHA03095 188 RSLLHHHL 195
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
659-771 |
4.24e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 659 IEYLVARKADASLADSSGQTPLHLFsmqriilkgsgeaaendaMRMTLDNYKKCFNTLIKAGAKVDVYDHEDNTPLHYAL 738
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLY------------------LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYL 91
|
90 100 110
....*....|....*....|....*....|....
gi 72001594 739 TNGN-LMLFNLMLDKVANKRnlfEKWANHQNFLH 771
Cdd:PHA03095 92 YNATtLDVIKLLIKAGADVN---AKDKVGRTPLH 122
|
|
| WGR |
cd07994 |
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ... |
1777-1840 |
4.26e-05 |
|
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: 43.42 E-value: 4.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72001594 1777 GFHNFYRMQIIKRRDAELFILFTNWGRIGSGMGEFQTTPFNSLELAAKEFKSIFKSKSGNEWAP 1840
Cdd:cd07994 10 GSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
350-442 |
5.40e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 43.95 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 350 LHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLLKNGGSvtMLTKQTETPLHVAARAGRAVNCT 429
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 72001594 430 FLMKEMLDLEKGD 442
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
526-682 |
6.14e-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: 48.26 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 526 EGKDKKK-RTPLIHAMLN---GQIHTAAFLL---AKGASL------TLADS--SGNTAAHYAAAYGFLDCLKLLAS--ID 588
Cdd:cd22196 40 EFKDPETgKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLkefvnaAYTDSyyKGQTALHIAIERRNMHLVELLVQngAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 589 DNILSEPNDWQL-----------YPLSVAYLKGHYGIVTWLLEGPHKdKANINAKDNNGATLLSNLLSYADET------- 650
Cdd:cd22196 120 VHARASGEFFKKkkggpgfyfgeLPLSLAACTNQLDIVKFLLENPHS-PADISARDSMGNTVLHALVEVADNTpentkfv 198
|
170 180 190
....*....|....*....|....*....|....
gi 72001594 651 --MHKELLSQIEYLVARKADASLADSSGQTPLHL 682
Cdd:cd22196 199 tkMYNEILILGAKIRPLLKLEEITNKKGLTPLKL 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
372-541 |
6.31e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.95 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 372 INIPDQDNWYT-MHYAACAPGTAPMEFLLKNGGSVTMLTKQTETPLHVAARAGRavnctflmkemldlekgDDGESTIRA 450
Cdd:PHA02878 160 INMKDRHKGNTaLHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN-----------------KPIVHILLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 451 DRSIINARTRSGNSALHLAVLR-NNLDVVDALLAEPTIVvdNPTSTGQNrLTPLMMACGKGylEMAKKLVEKGALVEGKD 529
Cdd:PHA02878 223 NGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV--NAKSYILG-LTALHSSIKSE--RKLKLLLEYGADINSLN 297
|
170
....*....|..
gi 72001594 530 KKKRTPLIHAML 541
Cdd:PHA02878 298 SYKLTPLSSAVK 309
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1438-1486 |
6.77e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 47.26 E-value: 6.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 72001594 1438 PISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVVDA 1486
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
|
|
| WGR_MMR_like |
cd07996 |
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ... |
1779-1833 |
1.09e-04 |
|
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: 42.59 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 72001594 1779 HNFYRMQIikrrDAELF---ILFTNWGRIGSGmGEFQTTPFNSLELAAKEFKSIFKSK 1833
Cdd:cd07996 14 ARFYEIEL----EGDLFgewSLVRRWGRIGTK-GQSRTKTFDSEEEALKAAEKLIREK 66
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1438-1491 |
1.11e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 46.49 E-value: 1.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 72001594 1438 PISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVVDAIVGDG 1491
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1439-1488 |
1.18e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.80 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 72001594 1439 ISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVVDAIV 1488
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1123-1174 |
1.40e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 72001594 1123 RPEQIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALA 1174
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1134-1187 |
1.62e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 72001594 1134 GNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVHHGRQSSALTLI 1187
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1051-1164 |
3.10e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.64 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1051 LHVAtlACDGSADSVLEpiaWLSTRCPIDAVDKFNRTALHYA--FGNENdfkegnvpfgesdpiaVVSLLSSLIRPEqie 1128
Cdd:pfam12796 1 LHLA--AKNGNLELVKL---LLENGADANLQDKNGRTALHLAakNGHLE----------------IVKLLLEHADVN--- 56
|
90 100 110
....*....|....*....|....*....|....*.
gi 72001594 1129 iADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKN 1164
Cdd:pfam12796 57 -LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| TCCD_inducible_PARP_like |
cd01439 |
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ... |
2083-2145 |
3.52e-04 |
|
Poly(ADP-ribose) polymerases catalyse 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. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation
Pssm-ID: 238719 [Multi-domain] Cd Length: 121 Bit Score: 42.31 E-value: 3.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72001594 2083 LWHGTKATNLMSILKNGFliDPPSACKNGNLFGSGIYLADSFEKSTHYCQ--PSAGGINYMLVCQ 2145
Cdd:cd01439 2 LFHGTSADAVEAICRHGF--DRRFCGKHGTMYGKGSYFAKNASYSHQYSKksPKADGLKEMFLAR 64
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
392-562 |
3.63e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 46.01 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 392 TAPMEFLLKNGGSVTMLTKQTETPLHVAARAGRAVNCTFLMKEMLDlekgddgestiradrsiINARTRSGNSALHLAVL 471
Cdd:PLN03192 538 AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN-----------------VHIRDANGNTALWNAIS 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 472 RNNLDVVDALLAEPTIvvDNPTSTGQnrltPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFL 551
Cdd:PLN03192 601 AKHHKIFRILYHFASI--SDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
|
170
....*....|.
gi 72001594 552 LAKGASLTLAD 562
Cdd:PLN03192 675 IMNGADVDKAN 685
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
491-539 |
4.04e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 4.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 72001594 491 NPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHA 539
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
659-756 |
4.37e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.25 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 659 IEYLVARKADASLADSSGQTPLHLfsmqriilkgsgeAAENdamrmtldNYKKCFNTLIKaGAKVDVYDHeDNTPLHYAL 738
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHL-------------AAKN--------GHLEIVKLLLE-HADVNLKDN-GRTALHYAA 69
|
90
....*....|....*...
gi 72001594 739 TNGNLMLFNLMLDKVANK 756
Cdd:pfam12796 70 RSGHLEIVKLLLEKGADI 87
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1138-1196 |
5.57e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.87 E-value: 5.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1138 LHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAVHHGRQSSALTLIQ-ANADVTEK 1196
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDN 60
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1438-1493 |
5.99e-04 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 44.17 E-value: 5.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 1438 PISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVVDAIVGDGKL 1493
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
510-682 |
6.83e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 44.87 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 510 GYLEMAKKLVEKGALVEGKDKKkrTPLIHAMLN---GQIHTAAFLL----AKGASLTLADSS-------GNTAAHYAAAY 575
Cdd:cd21882 6 GLLECLRWYLTDSAYQRGATGK--TCLHKAALNlndGVNEAIMLLLeaapDSGNPKELVNAPctdefyqGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 576 GFLDCLKLLASIDDNILSEPND------------WQLYPLSVAYLKGHYGIVTWLLEGPHkDKANINAKDNNGATLLSNL 643
Cdd:cd21882 84 RNLNLVRLLVENGADVSARATGrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGA-QPAALEAQDSLGNTVLHAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 72001594 644 LSYADET---------MHKELLSQIEYLVARKADASLADSSGQTPLHL 682
Cdd:cd21882 163 VLQADNTpensafvcqMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKL 210
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
1101-1181 |
7.08e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 44.86 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1101 EGNVPFGESDPIAVVS-----LLSSLIRPEQ-IEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALA 1174
Cdd:PLN03192 519 EHDDPNMASNLLTVAStgnaaLLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
|
....*..
gi 72001594 1175 VHHGRQS 1181
Cdd:PLN03192 599 ISAKHHK 605
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
511-682 |
7.19e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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: 411981 [Multi-domain] Cd Length: 640 Bit Score: 44.85 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 511 YLEMAKKLVEKGALVEGKDKKkrTPLIHAMLN---GQIHTAAFLLA----KGASLTLADSS-------GNTAAHYAAAYG 576
Cdd:cd22197 28 YLRRTSKYLTDSEYTEGSTGK--TCLMKAVLNlqdGVNACIMPLLEidkdSGNPKPLVNAQctdeyyrGHSALHIAIEKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 577 FLDCLKLL--------ASIDDNILSEPNDWQLY----PLSVAYLKGHYGIVTWLLEGPHkDKANINAKDNNGATLLSNLL 644
Cdd:cd22197 106 SLQCVKLLvengadvhARACGRFFQKKQGTCFYfgelPLSLAACTKQWDVVNYLLENPH-QPASLQAQDSLGNTVLHALV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 72001594 645 SYADET---------MHKELLSQIEYLVARKADASLADSSGQTPLHL 682
Cdd:cd22197 185 MIADNSpensalvikMYDGLLQAGARLCPTVQLEEISNHEGLTPLKL 231
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
414-482 |
1.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 72001594 414 TPLHVAARAGRavnctflmKEMLD--LEKGDDgestiradrsiINARTRSGNSALHLAVLRNNLDVVDALL 482
Cdd:pfam13637 3 TALHAAAASGH--------LELLRllLEKGAD-----------INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
515-586 |
1.14e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.12 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72001594 515 AKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGFLDCLKLLAS 586
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1437-1484 |
2.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 2.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 72001594 1437 PPISFAVLQENPNMIRALRNAGASLKTQDDYGRTPLMYAIMTNNRSVV 1484
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
349-584 |
3.03e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.56 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 349 PLHTAAISNSTHMLEAMRAVYPTINIPDQDNWYTMHYAACAPGTAPMEFLL--KNGGSVTMLTKQTETPLHvaaraGRAV 426
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsINKCSVFYTLVAIKDAFN-----NRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 427 NctflMKEMLdLEKGDDGESTIradrSIINARTRSGNSALHLAVLRnnldVVDALLAEPTIVVDNPTSTgqnrltPLMMA 506
Cdd:PHA02878 115 E----IFKII-LTNRYKNIQTI----DLVYIDKKSKDDIIEAEITK----LLLSYGADINMKDRHKGNT------ALHYA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 507 CGKGYLEMAKKLVEKGALVEGKDKKKRTPLIHAMLNGQIHTAAFLLAKGASLTLADSSGNTAAHYAAAYGF-LDCLKLL 584
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLL 254
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
456-570 |
3.84e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.38 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 456 NARTRSGNSALHLAVLrNNLDVVDALLA----------EPTIVVDNPTSTGQNRLTPLMMACGKGYLEMAKKLVEKGALV 525
Cdd:TIGR00870 76 SCRGAVGDTLLHAISL-EYVDAVEAILLhllaafrksgPLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASV 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 526 EGK------DKKKRTPLIH---AMLN-----GQIHTAAFLLAKGASLTLADSSGNTAAH 570
Cdd:TIGR00870 155 PARacgdffVKSQGVDSFYhgeSPLNaaaclGSPSIVALLSEDPADILTADSLGNTLLH 213
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1032-1175 |
4.04e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.96 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1032 KMIESKGVR-RETNDDGRSVLHVATLACDGSADSVLEpiaWLSTRCPIDAVDKFNRTALHYAF-GNENDFK------EGN 1103
Cdd:PHA03100 90 KLLLEYGANvNAPDNNGITPLLYAISKKSNSYSIVEY---LLDNGANVNIKNSDGENLLHLYLeSNKIDLKilklliDKG 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 72001594 1104 VpfgESDPIAVVSLLSSLIRPeqIEIADVNGNTILHLAAIKNSTICLMTLIRKKCHVDLKNKDGNTPLALAV 1175
Cdd:PHA03100 167 V---DINAKNRVNYLLSYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
602-767 |
5.09e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 41.99 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 602 PLSVAYLKGHYGIVTWLLEgphkDKANINAKDNNGATLLSnllSYADETMHKEL----------LSQIEYLVARKADASL 671
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLE----RGASVPARACGDFFVKS---QGVDSFYHGESplnaaaclgsPSIVALLSEDPADILT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 672 ADSSGQTPLHLFSMQriilkgSGEAAENDAMRMTldnykkCFNTLIKAGAKVD-------VYDHEDNTPLHYALTNGNLM 744
Cdd:TIGR00870 204 ADSLGNTLLHLLVME------NEFKAEYEELSCQ------MYNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIV 271
|
170 180
....*....|....*....|...
gi 72001594 745 LFNLMLDKVANKRNlFEKWANHQ 767
Cdd:TIGR00870 272 LFRLKLAIKYKQKK-FVAWPNGQ 293
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
533-682 |
5.19e-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: 42.09 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 533 RTPLIHAMLN---GQIHTAAFLLAKG-----------ASLTLADSSGNTAAHYAAAYGFLDCLKLL--ASIDDNILS--- 593
Cdd:cd22193 30 KTCLMKALLNlnpGTNDTIRILLDIAektdnlkrfinAEYTDEYYEGQTALHIAIERRQGDIVALLveNGADVHAHAkgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 594 --EPNDWQLY------PLSVAYLKGHYGIVTWLLEGPHKDkANINAKDNNGATLLSNLLSYADET---------MHKELL 656
Cdd:cd22193 110 ffQPKYQGEGfyfgelPLSLAACTNQPDIVQYLLENEHQP-ADIEAQDSRGNTVLHALVTVADNTkentkfvtrMYDMIL 188
|
170 180
....*....|....*....|....*.
gi 72001594 657 SQIEYLVARKADASLADSSGQTPLHL 682
Cdd:cd22193 189 IRGAKLCPTVELEEIRNNDGLTPLQL 214
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1414-1491 |
5.65e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 5.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72001594 1414 NIDALCQLEIPGKFKKILDYGLIPPISFAVLQENPNMIRALRNAGASlkTQDDYGRTPLMYAIMTNNRSVVDAIVGDG 1491
Cdd:pfam12796 9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKG 84
|
|
| WGR |
COG3831 |
WGR domain, predicted DNA-binding domain in MolR [Transcription]; |
1781-1833 |
7.19e-03 |
|
WGR domain, predicted DNA-binding domain in MolR [Transcription];
Pssm-ID: 443043 Cd Length: 83 Bit Score: 37.66 E-value: 7.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 72001594 1781 FYRMQIikrrDAELF---ILFTNWGRIGSgMGEFQTTPFNSLELAAKEFKSIFKSK 1833
Cdd:COG3831 17 FYELEV----EPDLFggwSLTRRWGRIGT-KGQTKTKTFASEEEALAALEKLVAEK 67
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
983-1194 |
7.76e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.16 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 983 IMYMIEMRMWELIPKVNASSEfwkSKDAKGNSVWH-YAARVNSHKTVGLFkMIESKGVRRETNDDGRSVLHVATlacdGS 1061
Cdd:PHA03095 91 LYNATTLDVIKLLIKAGADVN---AKDKVGRTPLHvYLSGFNINPKVIRL-LLRKGADVNALDLYGMTPLAVLL----KS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1062 ADSVLEPIAWL-STRCPIDAVDKFNRTALHYAFgneNDFKEGNvpfgesdpiavvSLLSSLIRPEQIEIA-DVNGNTILH 1139
Cdd:PHA03095 163 RNANVELLRLLiDAGADVYAVDDRFRSLLHHHL---QSFKPRA------------RIVRELIRAGCDPAAtDMLGNTPLH 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 72001594 1140 LAAIKNS--TICLMTLIRKKCHVDLKNKDGNTPLALAVHHGRQSSALTLIQANADVT 1194
Cdd:PHA03095 228 SMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
966-1191 |
7.81e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.10 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 966 HNAIKENELEVVvhKTIIMYMIEMRMwelipkvnassefwksKDAKGNSVWHYAARVNSHKTVglfKMIESKGVRRETND 1045
Cdd:PHA02874 129 HYAIKKGDLESI--KMLFEYGADVNI----------------EDDNGCYPIHIAIKHNFFDII---KLLLEKGAYANVKD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 1046 -DGRSVLHVATLACD-GSADSVLEPIAWLSTRCpidavdKFNRTALHYAFgnendfkegnvpfgesdpIAVVSLLSSLIR 1123
Cdd:PHA02874 188 nNGESPLHNAAEYGDyACIKLLIDHGNHIMNKC------KNGFTPLHNAI------------------IHNRSAIELLIN 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72001594 1124 PEQIEIADVNGNTILHLAAIKNSTICLM-TLIRKKCHVDLKNKDGNTPLALAVHHGRQSSALTLIQANA 1191
Cdd:PHA02874 244 NASINDQDIDGSTPLHHAINPPCDIDIIdILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANA 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
702-754 |
9.20e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.40 E-value: 9.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 72001594 702 MRMTLDNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNGNLMLFNLMLDKVA 754
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
623-749 |
9.76e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.01 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72001594 623 HKDKANINAKD----NNG----ATLLSNLLSYAdeTMHKELLsqIEYLVARKADASLADSSGQTPLHLfsmqriilkgsg 694
Cdd:PLN03192 501 HKELHDLNVGDllgdNGGehddPNMASNLLTVA--STGNAAL--LEELLKAKLDPDIGDSKGRTPLHI------------ 564
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 72001594 695 eAAENdamrmtldNYKKCFNTLIKAGAKVDVYDHEDNTPLHYALTNGNLMLFNLM 749
Cdd:PLN03192 565 -AASK--------GYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
|
| |
