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Conserved domains on  [gi|2470810270|ref|NP_001406157|]
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protein phosphatase 1 regulatory subunit 12C isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 684-783 4.15e-40

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


:

Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 142.83  E-value: 4.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 684 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 762
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 2470810270 763 DNQRLKDENAALIRVISKLSK 783
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-326 5.27e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 5.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL 173
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 174 PLDLAesdAMEGllkaeitrrgvDVEAAKraeeeLLlhdtrcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQA 253
Cdd:COG0666   156 PLHLA---AANG-----------NLEIVK-----LL-------LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEA 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2470810270 254 GYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADEDVMNLLEELAQKQEDLRNQK 326
Cdd:COG0666   209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.44e-26

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


:

Pssm-ID: 412020  Cd Length: 54  Bit Score: 102.86  E-value: 1.44e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2470810270 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 577
Cdd:cd21945     1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 508-697 4.09e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 508 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 587
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 588 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 667
Cdd:PRK12678  133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                         170       180       190
                  ....*....|....*....|....*....|
gi 2470810270 668 DlvlESKQEHEEPDGGFRKMYTELRRENER 697
Cdd:PRK12678  212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 684-783 4.15e-40

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 142.83  E-value: 4.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 684 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 762
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 2470810270 763 DNQRLKDENAALIRVISKLSK 783
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-326 5.27e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 5.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL 173
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 174 PLDLAesdAMEGllkaeitrrgvDVEAAKraeeeLLlhdtrcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQA 253
Cdd:COG0666   156 PLHLA---AANG-----------NLEIVK-----LL-------LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEA 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2470810270 254 GYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADEDVMNLLEELAQKQEDLRNQK 326
Cdd:COG0666   209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.44e-26

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 102.86  E-value: 1.44e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2470810270 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 577
Cdd:cd21945     1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
99-164 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270  99 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 164
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-272 4.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 114 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 185
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 186 LLKaeitrRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGW 265
Cdd:PHA03100  162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                  ....*..
gi 2470810270 266 TPLHAAA 272
Cdd:PHA03100  227 TPLHIAI 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-164 3.57e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.81  E-value: 3.57e-07
                           10        20
                   ....*....|....*....|....*...
gi 2470810270  137 EGWTPLHVAASCGYLDIARYLLSHGANI 164
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-274 6.66e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.78  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 170
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 171 GDlplDLAESDAMEGLLKAEITrrgvdvEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 242
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAEYE------ELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2470810270 243 YIEVMRLLLQAGYdtELRDGDGWT--PLHAAAHW 274
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 105-286 2.03e-06

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: 51.42  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 171
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 172 dlplDLAESDAMEGLLkaEITRRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 250
Cdd:cd21882   152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2470810270 251 LQ----AGYDTELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 286
Cdd:cd21882   224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
690-783 3.55e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 690 ELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQRL 767
Cdd:COG2433   424 RLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLERL 498

                          90       100
                  ....*....|....*....|...
gi 2470810270 768 KD-------ENAALIRVISKLSK 783
Cdd:COG2433   499 KElwklehsGELVPVKVVEKFTK 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 684-783 1.53e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  684 FRKMYTELRRENERLREALTETTLRLAQL-------KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKA 756
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLerriaatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEA 877

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2470810270  757 LSDLRADNQR----LKDENAALIRVISKLSK 783
Cdd:TIGR02168  878 LLNERASLEEalalLRSELEELSEELRELES 908
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 508-697 4.09e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 508 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 587
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 588 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 667
Cdd:PRK12678  133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                         170       180       190
                  ....*....|....*....|....*....|
gi 2470810270 668 DlvlESKQEHEEPDGGFRKMYTELRRENER 697
Cdd:PRK12678  212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
PTZ00121 PTZ00121
MAEBL; Provisional
 607-776 5.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  607 AQRAEAPEGQGQGPQAAREHRKAGHERRG--PAEGEEAGPAERSPECSTVDGGSQVRRQHSQRDLvlESKQEHEEPDGGF 684
Cdd:PTZ00121  1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMA 1579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  685 RKMYTELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKALSDLRADN 764
Cdd:PTZ00121  1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE---LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                          170
                   ....*....|..
gi 2470810270  765 QRLKDENAALIR 776
Cdd:PTZ00121  1657 EENKIKAAEEAK 1668
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 684-783 4.15e-40

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 142.83  E-value: 4.15e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 684 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 762
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 2470810270 763 DNQRLKDENAALIRVISKLSK 783
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-326 5.27e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 5.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL 173
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 174 PLDLAesdAMEGllkaeitrrgvDVEAAKraeeeLLlhdtrcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQA 253
Cdd:COG0666   156 PLHLA---AANG-----------NLEIVK-----LL-------LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEA 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2470810270 254 GYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADEDVMNLLEELAQKQEDLRNQK 326
Cdd:COG0666   209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-324 1.06e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL 173
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 174 PLDLAesdAMEGllkaeitrrgvDVEAAKraeeeLLlhdtrcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQA 253
Cdd:COG0666   123 PLHLA---AYNG-----------NLEIVK-----LL-------LEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 254 GYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA-----DEDVMNLLEELAQKQEDLRN 324
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengnLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-210 1.15e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 1.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  58 LAACAGGDLDEARLMLRA-ADPgpgsgaasdpavppparavlDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADN 136
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAgADV--------------------NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2470810270 137 EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEITRRGVDVEAAKRAEEELLL 210
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 524-577 1.44e-26

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 102.86  E-value: 1.44e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2470810270 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 577
Cdd:cd21945     1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-208 5.47e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 5.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  35 AGADPGPGERRARTVrferaaeFLAACAGGDLDEARLMLRA-ADPgpgsgaasdpavppparavlDSTNADGISALHQAC 113
Cdd:COG0666   142 AGADVNAQDNDGNTP-------LHLAAANGNLEIVKLLLEAgADV--------------------NARDNDGETPLHLAA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 114 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEITR 193
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                         170
                  ....*....|....*
gi 2470810270 194 RGVDVEAAKRAEEEL 208
Cdd:COG0666   275 LLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
99-164 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270  99 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 164
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 527-573 3.60e-17

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 75.46  E-value: 3.60e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2470810270 527 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 573
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-261 8.51e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 109 LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHganiAAVNSDGDlpldlaesdamegllk 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN---------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2470810270 189 aeitrrgvdveaakraeeelllhdtrcwlnggampearhprtGASALHVAAAKGYIEVMRLLLQAGYDTELRD 261
Cdd:pfam12796  61 ------------------------------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 524-577 8.55e-17

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412019  Cd Length: 57  Bit Score: 74.94  E-value: 8.55e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2470810270 524 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 577
Cdd:cd21944     3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-272 4.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 114 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 185
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 186 LLKaeitrRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGW 265
Cdd:PHA03100  162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                  ....*..
gi 2470810270 266 TPLHAAA 272
Cdd:PHA03100  227 TPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-310 2.34e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDSTNADGISALH-QACIDENLEVVRFLVEQGATVNQADNEGWTPLHVaascgYL-------DIARYLLSHGANIA 165
Cdd:PHA03095   72 AGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsgfninpKVIRLLLRKGADVN 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 166 AVNSDGDLPLD--LAESDAMEGLLKAEItRRGVDVeAAKRAEEELLLH--------DTRC---WLNGGAMPEARHpRTGA 232
Cdd:PHA03095  147 ALDLYGMTPLAvlLKSRNANVELLRLLI-DAGADV-YAVDDRFRSLLHhhlqsfkpRARIvreLIRAGCDPAATD-MLGN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 233 SALHVAAAKGYIE--VMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLAdedVMN 310
Cdd:PHA03095  224 TPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM---VRN 300
Ank_2 pfam12796
Ankyrin repeats (3 copies);
235-286 1.00e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.00e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2470810270 235 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-158 3.94e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 3.94e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2470810270 107 SALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLL 158
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 525-574 9.48e-13

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and similar proteins; Protein phosphatase 1 regulatory subunit 12A-like (PPP1R12A-like) is a homolog of MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit. MYPT1 is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of PPP1R12A-like protein.


Pssm-ID: 412022  Cd Length: 50  Bit Score: 63.35  E-value: 9.48e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2470810270 525 DSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKV 574
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 527-573 1.95e-12

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, also called protein phosphatase 1 regulatory subunit 12B (PPP1R12B), or myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. This model corresponds to the inhibitory phosphorylation domain of MYPT2.


Pssm-ID: 412021  Cd Length: 53  Bit Score: 62.37  E-value: 1.95e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2470810270 527 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 573
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAER 47
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 95-178 3.62e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  95 RAVLDSTNADGISALHQA--CIDENLEVVRFLVEQGATVNQ----------------ADNEGWTPLHVAASCGYLDIARY 156
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKY 210

                          90       100
                  ....*....|....*....|..
gi 2470810270 157 LLSHGANIAAVNSDGDLPLDLA 178
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-304 7.45e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 118 LEVVRFLVEQGATVNQADNEGWTPLHVAASCG---YLDIARYLLSHGANIAAVNSDGDLPLDL-----AESDAMEGLLK- 188
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLylynaTTLDVIKLLIKa 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 189 -AEIT----------------------------RRGVDVEA--------------AKRAEEELLlhdtRCWLNGGAMPEA 225
Cdd:PHA03095  107 gADVNakdkvgrtplhvylsgfninpkvirlllRKGADVNAldlygmtplavllkSRNANVELL----RLLIDAGADVYA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 226 RHPRtGASALHVAA--AKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGvedACRL-----LAEHGGGMDSLTHAGQ 298
Cdd:PHA03095  183 VDDR-FRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKRslvlpLLIAGISINARNRYGQ 258


                  ....*.
gi 2470810270 299 RPCDLA 304
Cdd:PHA03095  259 TPLHYA 264
Ank_4 pfam13637
Ankyrin repeats (many copies);
233-283 2.52e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2470810270 233 SALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLL 283
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 103-314 2.68e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 103 ADGISA-----LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLS------------------ 159
Cdd:PHA02878   30 STSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdaf 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 160 HGANIAAVNS------DGDLPLDLAESD--AMEGLLKAEITR----RGVDVEAAKRAEEELLLHD---------TRCWLN 218
Cdd:PHA02878  110 NNRNVEIFKIiltnryKNIQTIDLVYIDkkSKDDIIEAEITKlllsYGADINMKDRHKGNTALHYatenkdqrlTELLLS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 219 GGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVE-DACRLLAEHGGGMDSLTHA- 296
Cdd:PHA02878  190 YGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYIl 268

                         250       260
                  ....*....|....*....|
gi 2470810270 297 GQRPCDLA--DEDVMNLLEE 314
Cdd:PHA02878  269 GLTALHSSikSERKLKLLLE 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-178 2.84e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.20  E-value: 2.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 124 LVEQG-ATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 178
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 124-320 8.42e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 8.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 124 LVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLdlaesdamegllkaeitrrgVDVEAAKR 203
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL--------------------WNAISAKH 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 204 AEEELLLHDtrcwlnggaMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLL 283
Cdd:PLN03192  604 HKIFRILYH---------FASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2470810270 284 AEHGGGMDslthagqrpCDLADEDVMNL-LEELAQKQE 320
Cdd:PLN03192  675 IMNGADVD---------KANTDDDFSPTeLRELLQKRE 703
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 98-169 5.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 5.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2470810270  98 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNS 169
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 119-304 6.34e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 6.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 119 EVVRFLVEQGATVNQAD-NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAeitrrgvd 197
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI-------- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 198 veaakraeeelllhdtrcWLNGGAMPEARHpRTGASALHVAAakGY---IEVMRLLLQAGYDTELRDG-DGWTPLHAAAH 273
Cdd:PHA02878  220 ------------------LLENGASTDARD-KCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2470810270 274 wgVEDACRLLAEHGGGMDSLTHAGQRPCDLA 304
Cdd:PHA02878  279 --SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-179 2.50e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  34 RAGADPGPGERRARTVRFERAAEFLAACAggDLDEARLMLRAADpgpgsGAASDPAVPPPARAVLDSTNADGISA-LHQA 112
Cdd:PTZ00322   17 LFFGTEGSRKRRAKPISFERMAAIQEEIA--RIDTHLEALEATE-----NKDATPDHNLTTEEVIDPVVAHMLTVeLCQL 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2470810270 113 CIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAE 179
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-168 5.02e-08

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 49.21  E-value: 5.02e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2470810270 137 EGWTPLHVAA-SCGYLDIARYLLSHGANIAAVN 168
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 105-286 1.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAME 184
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKD 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 185 GLLKAEITRRGVDVEaakrAEEELLlhdtrcwlnggampearhprtGASALHVAAAKGyiEVMRLLLQAGYDTELRDGDG 264
Cdd:PHA02878  248 YDILKLLLEHGVDVN----AKSYIL---------------------GLTALHSSIKSE--RKLKLLLEYGADINSLNSYK 300

                         170       180
                  ....*....|....*....|....
gi 2470810270 265 WTPLHAAA--HWGVEdACRLLAEH 286
Cdd:PHA02878  301 LTPLSSAVkqYLCIN-IGRILISN 323
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 137-164 3.57e-07

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.81  E-value: 3.57e-07
                           10        20
                   ....*....|....*....|....*...
gi 2470810270  137 EGWTPLHVAASCGYLDIARYLLSHGANI 164
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-301 5.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  94 ARAVLDS------TNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAV 167
Cdd:PHA02875   18 ARRLLDIginpnfEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 168 -NSDGDLPLDLA----ESDAMEGLLKaeitrRGVDVEAakraeeelllhdtrcwlnggampearhPRTG-ASALHVAAAK 241
Cdd:PHA02875   98 fYKDGMTPLHLAtilkKLDIMKLLIA-----RGADPDI---------------------------PNTDkFSPLHLAVMM 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 242 GYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDsltHAGQRPC 301
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGC 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
138-178 5.72e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.72e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2470810270 138 GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 178
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 117-229 6.08e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 117 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL-PLDLAESdamegLLKAEITRRG 195
Cdd:PLN03192  634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTELREL-----LQKRELGHSI 708

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2470810270 196 VDVEAAKRAEEELLL--HDTRCWLNGGAMPEARHPR 229
Cdd:PLN03192  709 TIVDSVPADEPDLGRdgGSRPGRLQGTSSDNQCRPR 744
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-274 6.66e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.78  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 170
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 171 GDlplDLAESDAMEGLLKAEITrrgvdvEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 242
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAEYE------ELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2470810270 243 YIEVMRLLLQAGYdtELRDGDGWT--PLHAAAHW 274
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 99-175 1.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2470810270  99 DSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPL 175
Cdd:PHA02875  129 DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 117-287 1.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 117 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAvnsdgdLPLDLAESDAMEGLLKAeitrrGV 196
Cdd:PHA02874   47 DAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCIEKDMIKTILDC-----GI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 197 DVEAAKRAEEELL--------LHDTRCWLNGGAMPEARHPrTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPL 268
Cdd:PHA02874  116 DVNIKDAELKTFLhyaikkgdLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         170
                  ....*....|....*....
gi 2470810270 269 HAAAHWGVEDACRLLAEHG 287
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHG 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 98-315 2.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  98 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDL 177
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 178 AesdamegllkaeitrrgvdVEAAKRAEEELLLHDTRCWLNggampearHPRTGASALHVAAAKGYIEVMRLLLQAGYDT 257
Cdd:PHA02874  197 A-------------------AEYGDYACIKLLIDHGNHIMN--------KCKNGFTPLHNAIIHNRSAIELLINNASIND 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2470810270 258 ElrDGDGWTPLHAAAHWGVE-DACRLLAEHGGGMDSLTHAGQRPCDLADEDV--MNLLEEL 315
Cdd:PHA02874  250 Q--DIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYInkDPVIKDI 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-178 2.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  95 RAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLP 174
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226


                  ....
gi 2470810270 175 LDLA 178
Cdd:PHA02874  227 LHNA 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 105-286 2.03e-06

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: 51.42  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 171
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 172 dlplDLAESDAMEGLLkaEITRRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 250
Cdd:cd21882   152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2470810270 251 LQ----AGYDTELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 286
Cdd:cd21882   224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-160 2.31e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  54 AAEFLAACAGGDLDEARLMLraadpgpgSGAAsDPavppparavlDSTNADGISALHQACIDENLEVVRFLVEQGATVNQ 133
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILL--------TGGA-DP----------NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143

                          90       100
                  ....*....|....*....|....*..
gi 2470810270 134 ADNEGWTPLHVAASCGYLDIARYLLSH 160
Cdd:PTZ00322  144 LDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 214-286 2.88e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2470810270 214 RCWLNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 286
Cdd:PTZ00322   99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 137-166 5.23e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.40  E-value: 5.23e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2470810270 137 EGWTPLHVAASCGYLDIARYLLSHGANIAA 166
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
229-271 5.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2470810270 229 RTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAA 271
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 108-291 1.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 108 ALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGAnIAAVNSDGdlpldlAESDAMEGLL 187
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPD------IESELHDAVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 188 KAEItrrgvdveaakRAEEELLLHDTrcWLNGGAMpearhpRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTP 267
Cdd:PHA02875   78 EGDV-----------KAVEELLDLGK--FADDVFY------KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                         170       180
                  ....*....|....*....|....
gi 2470810270 268 LHAAAHWGVEDACRLLAEHGGGMD 291
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLD 162
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 95-272 2.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  95 RAVLDS---TNADGISALhQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLD-IARYLLSHGANIAAVNSD 170
Cdd:PHA02876  228 KAIIDNrsnINKNDLSLL-KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 171 GDLPLDLAESDAMEGLLKAEITRRGVDVEAAKRaeeellLHDTrcwlnggampearhPRTGASALhvaaaKGYIEVMRLL 250
Cdd:PHA02876  307 GETPLYLMAKNGYDTENIRTLIMLGADVNAADR------LYIT--------------PLHQASTL-----DRNKDIVITL 361

                         170       180
                  ....*....|....*....|..
gi 2470810270 251 LQAGYDTELRDGDGWTPLHAAA 272
Cdd:PHA02876  362 LELGANVNARDYCDKTPIHYAA 383
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-312 2.50e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 186 LLKAEITRRGVDVEAAKRAEEELLLHDTRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGW 265
Cdd:COG0666     9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2470810270 266 TPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA----DEDVMNLL 312
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-145 2.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2470810270  98 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVA 145
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 105-175 3.14e-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: 47.31  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQA-----------DNE---GWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 170
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 2470810270 171 GDLPL 175
Cdd:cd22192   169 GNTVL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 239-341 4.14e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 239 AAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADE----DVMNLLEE 314
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEngfrEVVQLLSR 169

                          90       100
                  ....*....|....*....|....*..
gi 2470810270 315 LAQKQEDLRNQKEGSQGRGQESQVPSS 341
Cdd:PTZ00322  170 HSQCHFELGANAKPDSFTGKPPSLEDS 196
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-272 5.24e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 116 ENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAES----DAMEGLL--KA 189
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDskniDTIKAIIdnRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 190 EITRRGVDVEAAKRAEE---ELLLHDTRCWLNG----------------------------GAMPEARHPRtGASALHVA 238
Cdd:PHA02876  236 NINKNDLSLLKAIRNEDletSLLLYDAGFSVNSiddckntplhhasqapslsrlvpkllerGADVNAKNIK-GETPLYLM 314

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2470810270 239 AAKGY-IEVMRLLLQAGYDTELRDGDGWTPLHAAA 272
Cdd:PHA02876  315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQAS 349
PHA02795 PHA02795
ankyrin-like protein; Provisional
 118-178 6.31e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 6.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2470810270 118 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 178
Cdd:PHA02795  201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 104-259 8.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 104 DGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAm 183
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG- 179

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 184 egllkaeitrrgvDVEAAkraeeelllhdtRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDTEL 259
Cdd:PHA02875  180 -------------DIAIC------------KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 97-178 9.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  97 VLDSTN------ADGISALHQACIdENLEVVRFLVEQgATVNQADNEGWTPLHVAAS--CGyLDIARYLLSHGANIAAVN 168
Cdd:PHA02874  209 LIDHGNhimnkcKNGFTPLHNAII-HNRSAIELLINN-ASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKD 285

                          90
                  ....*....|
gi 2470810270 169 SDGDLPLDLA 178
Cdd:PHA02874  286 NKGENPIDTA 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-132 1.09e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 2470810270 104 DGISALHQACIDENLEVVRFLVEQGATVN 132
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-136 1.17e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2470810270 104 DGISALHQACIDE-NLEVVRFLVEQGATVNQADN 136
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 118-171 1.96e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2470810270 118 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGY---LDIARYLLSHGANIAAVNSDG 171
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDG 145
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
690-783 3.55e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 690 ELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQRL 767
Cdd:COG2433   424 RLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLERL 498

                          90       100
                  ....*....|....*....|...
gi 2470810270 768 KD-------ENAALIRVISKLSK 783
Cdd:COG2433   499 KElwklehsGELVPVKVVEKFTK 521
Ank_2 pfam12796
Ankyrin repeats (3 copies);
59-135 3.77e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 3.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2470810270  59 AACAGGDLDEARLMLRAADpgpgsgaasdpavppparavLDSTNaDGISALHQACIDENLEVVRFLVEQGATVNQAD 135
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD--------------------VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 97-175 3.79e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.13  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  97 VLDSTNADGISALHQACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVAASCG--------------YLDIARYLLSH 160
Cdd:PHA02716  309 KLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISL 388

                          90
                  ....*....|....*
gi 2470810270 161 GANIAAVNSDGDLPL 175
Cdd:PHA02716  389 GADITAVNCLGYTPL 403
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 96-168 6.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 6.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2470810270  96 AVLDSTNADGISALHQA-CIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVN 168
Cdd:PHA02876  332 ADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 686-783 6.54e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 686 KMYTELRRENERLREALTETTLRLAQLKVELERATQRQERF-----AERPALLELERFERRALERKAAELEEELKALSDL 760
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                          90       100
                  ....*....|....*....|...
gi 2470810270 761 RADNQRLKDENAALIRVISKLSK 783
Cdd:COG4942   219 QQEAEELEALIARLEAEAAAAAE 241
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 105-175 6.88e-04

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: 43.26  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVN-QADNE-------------GWTPLHVAASCGYLDIARYLLSH---GANIAAV 167
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHaRASGEffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173


                  ....*...
gi 2470810270 168 NSDGDLPL 175
Cdd:cd22196   174 DSMGNTVL 181
PHA02798 PHA02798
ankyrin-like protein; Provisional
 115-175 7.93e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 7.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 115 DENLEVVRFLVEQGATVNQADNEGWTPLHVAASC-----GYLDIARYLLSHGANIAAVNSDGDLPL 175
Cdd:PHA02798   48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPL 113
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 105-269 9.12e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGAT-VNQADN----EGWTPLHvaascgyldiaryllshganIAAVNSDgdlpldlae 179
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALH--------------------IAVVNQN--------- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 180 sdamEGLLKAEItRRGVDVEAAkRAEEELLLHDTRCWLNGGampeaRHPrtgasaLHVAAAKGYIEVMRLLLQAGYDTEL 259
Cdd:cd22192   102 ----LNLVRELI-ARGADVVSP-RATGTFFRPGPKNLIYYG-----EHP------LSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|
gi 2470810270 260 RDGDGWTPLH 269
Cdd:cd22192   165 QDSLGNTVLH 174
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-261 1.13e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2470810270 231 GASALHVAAAK-GYIEVMRLLLQAGYDTELRD 261
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 662-781 1.14e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 662 RQHSQRDLVLESKQEHEEpdggfrKMYTELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFE-R 740
Cdd:COG1196   291 YELLAELARLEQDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaE 364

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2470810270 741 RALERKAAELEEELKALSDLRADNQRLKDENAALIRVISKL 781
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 105-252 1.22e-03

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: 42.15  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVN-QADNE------------GWTPLHVAASCGYLDIARYLLSHGANIAAV---N 168
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHaRACGRffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLqaqD 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 169 SDGDLPL--------DLAESDAMEGLLKAEITRRGVDVEAAKRAEEelllhdtrcwlnggaMPEarhpRTGASALHVAAA 240
Cdd:cd22197   174 SLGNTVLhalvmiadNSPENSALVIKMYDGLLQAGARLCPTVQLEE---------------ISN----HEGLTPLKLAAK 234

                         170
                  ....*....|..
gi 2470810270 241 KGYIEVMRLLLQ 252
Cdd:cd22197   235 EGKIEIFRHILQ 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-132 1.25e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.25e-03
                           10        20
                   ....*....|....*....|....*....
gi 2470810270  104 DGISALHQACIDENLEVVRFLVEQGATVN 132
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 684-783 1.53e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  684 FRKMYTELRRENERLREALTETTLRLAQL-------KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKA 756
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLerriaatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEA 877

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2470810270  757 LSDLRADNQR----LKDENAALIRVISKLSK 783
Cdd:TIGR02168  878 LLNERASLEEalalLRSELEELSEELRELES 908
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 112-175 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 112 ACIDE---NLEVVRFLVEQGATVN-QADNEGWTPLHvaascGYL--------DIARYLLSHGANIAAVNSDGDLPL 175
Cdd:PHA02859   57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALH-----HYLsfnknvepEILKILIDSGSSITEEDEDGKNLL 127
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 101-172 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 101 TNADGISALHQ-ACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVaascgYLD-------IARYLLSHGANIAAVNSD 170
Cdd:PHA02859   83 TRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-----YMCnfnvrinVIKLLIDSGVSFLNKDFD 157


                  ..
gi 2470810270 171 GD 172
Cdd:PHA02859  158 NN 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 659-782 2.23e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 659 QVRRQHSQRDLVLESKQEHEEpdggfrkmytELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERF 738
Cdd:COG1196   271 ELRLELEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEE 337

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2470810270 739 ERRALERKAAELEEELKALSDLRAD-NQRLKDENAALIRVISKLS 782
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELE 382
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-178 2.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2470810270 107 SALHQACIDEN-LEVVRFLVEQGATVNQADNEGWTPLHVAA--SCGyLDIARYLLSHGANIAAVNSDGDLPLDLA 178
Cdd:PHA02876  410 TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACkkNCK-LDVIEMLLDNGADVNAINIQNQYPLLIA 483
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 231-256 2.61e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.61e-03
                           10        20
                   ....*....|....*....|....*.
gi 2470810270  231 GASALHVAAAKGYIEVMRLLLQAGYD 256
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 697-774 2.91e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.53  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 697 RLREALTETTLR---LAQLKVELERATQRQERF--AERPALLELERfERRALERKAAELEEELKALSDLradNQRLKDEN 771
Cdd:pfam08614  61 QLREELAELYRSrgeLAQRLVDLNEELQELEKKlrEDERRLAALEA-ERAQLEEKLKDREEELREKRKL---NQDLQDEL 136


                  ...
gi 2470810270 772 AAL 774
Cdd:pfam08614 137 VAL 139
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 508-697 4.09e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 508 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 587
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 588 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 667
Cdd:PRK12678  133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                         170       180       190
                  ....*....|....*....|....*....|
gi 2470810270 668 DlvlESKQEHEEPDGGFRKMYTELRRENER 697
Cdd:PRK12678  212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 232-287 4.37e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 4.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2470810270 232 ASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHG 287
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 105-252 4.42e-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: 40.55  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 105 GISALHQACIDENLEVVRFLVEQGATVNQADNE--------------GWTPLHVAASCGYLDIARYLLSHG---ANIAAV 167
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270 168 NSDGDlpldlaesDAMEGLLK-AEITRRGVDVeaAKRAEEELLLHDTRcWLNGGAMPEARHpRTGASALHVAAAKGYIEV 246
Cdd:cd22193   156 DSRGN--------TVLHALVTvADNTKENTKF--VTRMYDMILIRGAK-LCPTVELEEIRN-NDGLTPLQLAAKMGKIEI 223


                  ....*.
gi 2470810270 247 MRLLLQ 252
Cdd:cd22193   224 LKYILQ 229
PTZ00121 PTZ00121
MAEBL; Provisional
 607-776 5.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  607 AQRAEAPEGQGQGPQAAREHRKAGHERRG--PAEGEEAGPAERSPECSTVDGGSQVRRQHSQRDLvlESKQEHEEPDGGF 684
Cdd:PTZ00121  1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA--EEAKKAEEDKNMA 1579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2470810270  685 RKMYTELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKALSDLRADN 764
Cdd:PTZ00121  1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE---LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656

                          170
                   ....*....|..
gi 2470810270  765 QRLKDENAALIR 776
Cdd:PTZ00121  1657 EENKIKAAEEAK 1668
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 263-287 7.83e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.83e-03
                          10        20
                  ....*....|....*....|....*.
gi 2470810270 263 DGWTPLHAAA-HWGVEDACRLLAEHG 287
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKG 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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