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Conserved domains on  [gi|568909313|ref|XP_006529770|]
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protein phosphatase 1 regulatory subunit 12B isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-290 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgriedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909313  222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 936-1043 5.78e-39

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: 140.13  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   936 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 1015
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                           90       100
                   ....*....|....*....|....*...
gi 568909313  1016 QIQTLKQMNEQLQAENRALTRVVARLSK 1043
Cdd:pfam15898   75 VLEDLRAENQRLKDENGALIRVISKLSK 102
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 669-724 6.58e-19

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: 81.49  E-value: 6.58e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313  669 SVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 724
Cdd:cd21944     2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 542-810 7.01e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.51  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   542 TIAPSTYTSTYLKSASFGKSSDPTSPYISANRN-SSPATSPITIGSSTSRGSQwQPASSCPAPVSTNTPAPVQHVRTPYK 620
Cdd:pfam17823   64 TAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDlSEPATREGAADGAASRALA-AAASSSPSSAAQSLPAAIAALPSEAF 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   621 SQADSTAEKTADSVSSSTPLCVI----TNRPAPSTANGVPAATVFSSAGTDPSVEAREKRRSYLTPVRD---------EE 687
Cdd:pfam17823  143 SAPRAAACRANASAAPRAAIAAAsaphAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGistaatatgHP 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   688 AESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSrSRAERQAQEQPGEKLEDPGGLEGSTKKQEPS-------AAPTKG 760
Cdd:pfam17823  223 AAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA-AAAGTVASAAGTINMGDPHARRLSPAKHMPSdtmarnpAAPMGA 301

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568909313   761 AGEGRSLE---EEPIYHRLRYPTqPDKPTTPVSPSASRPSLYTGSHLLRTSRA 810
Cdd:pfam17823  302 QAQGPIIQvstDQPVHNTAGEPT-PSPSNTTLEPNTPKSVASTNLAVVTTTKA 353
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 169-257 3.32e-03

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGRIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 568909313  233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-290 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgriedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909313  222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 936-1043 5.78e-39

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: 140.13  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   936 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 1015
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                           90       100
                   ....*....|....*....|....*...
gi 568909313  1016 QIQTLKQMNEQLQAENRALTRVVARLSK 1043
Cdd:pfam15898   75 VLEDLRAENQRLKDENGALIRVISKLSK 102
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.82e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313    65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANVNQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 568909313   145 SHGASVGIVN 154
Cdd:pfam12796   82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 2.52e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAAS------ 133
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfninp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  134 ------------------CGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKkqgvdleQSRKEEEQQM 195
Cdd:PHA03095  133 kvirlllrkgadvnaldlYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHL-------QSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  196 lqdaRQWLNSGRIEDVRQaRSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEAL 273
Cdd:PHA03095  206 ----RELIRAGCDPAATD-MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 568909313  274 CDMDIRNKLGQTPFDVA 290
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 669-724 6.58e-19

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: 81.49  E-value: 6.58e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313  669 SVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 724
Cdd:cd21944     2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-305 3.65e-08

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: 57.33  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   45 LQTRRGSprvrfeDGAVFLAAcSSGDTDEVKKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANVNQ--- 119
Cdd:cd22192    11 LQQKRIS------ESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmt 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  120 -QDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqd 198
Cdd:cd22192    84 sDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY------------------------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  199 arqwlnsgriedvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD 277
Cdd:cd22192   135 -----------------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYD 196

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568909313  278 ----------IRNKLGQTPFDVA-DEGLVEHLEMLQKKQ 305
Cdd:cd22192   197 keddlqpldlVPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 542-810 7.01e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.51  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   542 TIAPSTYTSTYLKSASFGKSSDPTSPYISANRN-SSPATSPITIGSSTSRGSQwQPASSCPAPVSTNTPAPVQHVRTPYK 620
Cdd:pfam17823   64 TAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDlSEPATREGAADGAASRALA-AAASSSPSSAAQSLPAAIAALPSEAF 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   621 SQADSTAEKTADSVSSSTPLCVI----TNRPAPSTANGVPAATVFSSAGTDPSVEAREKRRSYLTPVRD---------EE 687
Cdd:pfam17823  143 SAPRAAACRANASAAPRAAIAAAsaphAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGistaatatgHP 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   688 AESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSrSRAERQAQEQPGEKLEDPGGLEGSTKKQEPS-------AAPTKG 760
Cdd:pfam17823  223 AAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA-AAAGTVASAAGTINMGDPHARRLSPAKHMPSdtmarnpAAPMGA 301

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568909313   761 AGEGRSLE---EEPIYHRLRYPTqPDKPTTPVSPSASRPSLYTGSHLLRTSRA 810
Cdd:pfam17823  302 QAQGPIIQvstDQPVHNTAGEPT-PSPSNTTLEPNTPKSVASTNLAVVTTTKA 353
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-150 8.45e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 8.45e-05
                            10        20
                    ....*....|....*....|....*...
gi 568909313    123 EGWTPLHAAASCGYLNIAEYFISHGASV 150
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 939-1048 2.54e-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: 44.75  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  939 KLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEktsdrssVLEVEKRERRALERKMSEMEEEMKNLHqlKQIQ 1018
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                          90       100       110
                  ....*....|....*....|....*....|
gi 568909313 1019 TLKQMNEQLQAENRALTRVVARLSKSIESS 1048
Cdd:COG4942   210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 955-1046 4.89e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 44.17  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  955 LQEAQLELADIKAKLEKMAQQKQEktsdRSSVLEVEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA- 1033
Cdd:PRK11448  144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQk 217

                          90
                  ....*....|...
gi 568909313 1034 LTRVVARLSKSIE 1046
Cdd:PRK11448  218 RKEITDQAAKRLE 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 1.00e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313    91 GLTALHQACIDENLDMVKFLVENRANVNQQDN--------------EGWTPLHAAASCGYLNIAEYFISHGASVGIVNSE 156
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   157 G-EVPSDLAEEPAMKDL---LLEQVKKQGVD-LEQSRKEEEqqmlqdarqwlnsgrIEDVRQaRSGATALHVAAAKGYSE 231
Cdd:TIGR00870  208 GnTLLHLLVMENEFKAEyeeLSCQMYNFALSlLDKLRDSKE---------------LEVILN-HQGLTPLKLAAKEGRIV 271

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568909313   232 VLRLLIQAGYElnVQDHDGWT--PLHAAAHW 260
Cdd:TIGR00870  272 LFRLKLAIKYK--QKKFVAWPngQQLLSLYW 300
PHA03247 PHA03247
large tegument protein UL36; Provisional
 509-796 1.28e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  509 EKENRESAVNLVRSGSHTRQLWRdEAKGSETPQTIAPSTYTSTYLKSASFGKSSDPTSPYISANRNSSPATsPITIGSST 588
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGR-AAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSAT-PLPPGPAA 2727

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  589 SRGSQ-WQPASSCPAPVSTNTPAPVQhVRTPYKSQADSTAEKTA------------------DSVSSSTPLCVITNRPAP 649
Cdd:PHA03247 2728 ARQASpALPAAPAPPAVPAGPATPGG-PARPARPPTTAGPPAPAppaapaagpprrltrpavASLSESRESLPSPWDPAD 2806

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  650 STANGVPAA----TVFSSAGTDPSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 725
Cdd:PHA03247 2807 PPAAVLAPAaalpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909313  726 AERQAQEQPGEKLEDPGGLEGSTKKQEPSAAPTKGAGEGRSLEEEPiyhrLRYPTQPDKPTTPVSPSASRP 796
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----PPPPPRPQPPLAPTTDPAGAG 2953
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 3.32e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGRIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 568909313  233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 946-1050 9.63e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   946 TENQKLKTKLQEAQLELADIK----AKLEKMAQQKQEKTSDRSSVLEVEKRERralerkmsEMEEEMKNLHQ-----LKQ 1016
Cdd:TIGR04523  356 SENSEKQRELEEKQNEIEKLKkenqSYKQEIKNLESQINDLESKIQNQEKLNQ--------QKDEQIKKLQQekellEKE 427

                           90       100       110
                   ....*....|....*....|....*....|....
gi 568909313  1017 IQTLKQMNEQLQAENRALTRVVARLSKSIESSDT 1050
Cdd:TIGR04523  428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-290 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgriedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909313  222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 936-1043 5.78e-39

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: 140.13  E-value: 5.78e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   936 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 1015
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                           90       100
                   ....*....|....*....|....*...
gi 568909313  1016 QIQTLKQMNEQLQAENRALTRVVARLSK 1043
Cdd:pfam15898   75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-305 5.84e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 5.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgriedvrqarsgaTAL 221
Cdd:COG0666   138 LLLEAGADVNAQDNDGN------------------------------------------------------------TPL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-DEGLVEHLEM 300
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaENGNLEIVKL 237


                  ....*
gi 568909313  301 LQKKQ 305
Cdd:COG0666   238 LLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-215 1.58e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.15  E-value: 1.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   63 LAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEY 142
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909313  143 FISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQDARQWLNSGRIEDVRQAR 215
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.82e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.26  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313    65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANVNQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 568909313   145 SHGASVGIVN 154
Cdd:pfam12796   82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 2.52e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAAS------ 133
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfninp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  134 ------------------CGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKkqgvdleQSRKEEEQQM 195
Cdd:PHA03095  133 kvirlllrkgadvnaldlYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHL-------QSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  196 lqdaRQWLNSGRIEDVRQaRSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEAL 273
Cdd:PHA03095  206 ----RELIRAGCDPAATD-MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 568909313  274 CDMDIRNKLGQTPFDVA 290
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 669-724 6.58e-19

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: 81.49  E-value: 6.58e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313  669 SVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 724
Cdd:cd21944     2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 671-723 9.41e-19

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: 80.90  E-value: 9.41e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568909313  671 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 723
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-247 2.55e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.55e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313    95 LHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGasvgivnsegevpsdlaeepamkdlll 174
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568909313   175 eqvkkqgvdleqsrkeeeqqmlqdarqwlnsgrieDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 247
Cdd:pfam12796   54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-258 3.53e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 3.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   72 DEVKKLLARGADINTVNVDGLTALH-----QACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASC--GYLNIAEYFI 144
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  145 SHGASVGIVNSEGEVPSDLAEEPAMKDL-LLEQVKKQGVDLEQSRKEEeqqMLqdarqwLNSGRIEDVRQARsGATALHV 223
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKGVDINAKNRVN---YL------LSYGVPINIKDVY-GFTPLHY 198

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568909313  224 AAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAA 258
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 673-725 7.73e-18

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: 78.16  E-value: 7.73e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568909313  673 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 725
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 673-719 1.81e-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: 77.00  E-value: 1.81e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909313  673 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEK 719
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-164 1.07e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQA--CIDENLDMVKFLVENRANVNQQ----------------DNE 123
Cdd:PHA03100  112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVY 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568909313  124 GWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-144 1.78e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 71.54  E-value: 1.78e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568909313    91 GLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-301 2.74e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   221 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 299
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                   ..
gi 568909313   300 ML 301
Cdd:pfam12796   79 LL 80
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 671-720 6.75e-14

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: 66.82  E-value: 6.75e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568909313  671 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKT 720
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-290 1.23e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   70 DTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGAS 149
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  150 VGIVNSEGEVPSDLAEE---PAMKDLLLEqvkkqgvdleqsrkeeeqqmlqdarqwlNSGRIEDvrQARSGATALHVAAA 226
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEygdYACIKLLID----------------------------HGNHIMN--KCKNGFTPLHNAII 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909313  227 KGYSeVLRLLIQaGYELNVQDHDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02874  233 HNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-290 1.80e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   85 NTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  165 EEPA--MKDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQA 239
Cdd:PHA02878  111 NRNVeiFKIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568909313  240 GYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-290 4.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDnegwTPLHAAASCGYLNIAEYFI 144
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  145 SHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDleqsrkeeeqqmlqdarqwLNSGRIEdvrqarsGATALHVA 224
Cdd:PHA02876  261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGAD-------------------VNAKNIK-------GETPLYLM 314

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909313  225 AAKGY-SEVLRLLIQAGYELNVQDHDGWTPLHAAAHWG-VKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02876  315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA 382
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-155 7.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.54  E-value: 7.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   72 DEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVG 151
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ....
gi 568909313  152 IVNS 155
Cdd:PHA03100  253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-269 6.57e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 6.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568909313   219 TALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSIL 269
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 70-283 1.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   70 DTDEVKKLLARGADINTVNVDGL-TALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGA 148
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  149 SVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLeqsrkeeeqqmlqdarqwlnsgrieDVRQARSGATALHVAAAKg 228
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV-------------------------NAKSYILGLTALHSSIKS- 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909313  229 ySEVLRLLIQAGYELNVQDHDGWTPLHAAA--HWGVkEACSILAEALC-----DMDIRNKLG 283
Cdd:PHA02878  280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCI-NIGRILISNICllkriKPDIKNSEG 339
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 4.70e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.20  E-value: 4.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313    77 LLARG-ADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAA 131
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-121 5.31e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 5.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568909313    64 AACSSGDTDEVkKLLARGADINtVNVDGLTALHQACIDENLDMVKFLVENRANVNQQD 121
Cdd:pfam12796   36 LAAKNGHLEIV-KLLLEHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
61-111 8.36e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 8.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568909313    61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLV 111
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 6.05e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 6.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313   110 LVENR-ANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-292 6.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 6.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  103 NLDMVKFLVENRAN-VNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEgeVPSDL------AEEPAMKDLLLE 175
Cdd:PHA02874   13 DIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK--IPHPLltaikiGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  176 QVKKQGVDLEQSRKEEEQQMLQdarqwlnSGRIEDVRQARSgATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 255
Cdd:PHA02874   91 GVDTSILPIPCIEKDMIKTILD-------CGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568909313  256 AAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 292
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-159 7.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   54 VRFEDGAVFL-AACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAA 132
Cdd:PHA02875   97 VFYKDGMTPLhLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                          90       100
                  ....*....|....*....|....*..
gi 568909313  133 SCGYLNIAEYFISHGASVGIVNSEGEV 159
Cdd:PHA02875  177 AKGDIAICKMLLDSGANIDYFGKNGCV 203
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 63-169 1.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   63 LAAcsSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEY 142
Cdd:PTZ00322   89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568909313  143 FISH------GASVGIVNSEGEVPSDLAEEPAM 169
Cdd:PTZ00322  167 LSRHsqchfeLGANAKPDSFTGKPPSLEDSPIS 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 69-183 1.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   69 GDTDEVKKLLARGADINTVNVDGLTALHQACIdENLDMVKFLVENRAnVNQQDNEGWTPLHAAAS--CGyLNIAEYFISH 146
Cdd:PHA02874  201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLINNAS-INDQDIDGSTPLHHAINppCD-IDIIDILLYH 277

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568909313  147 GASVGIVNSEGEVPSDLA-----EEPAMKDLLLEQVKKQGVD 183
Cdd:PHA02874  278 KADISIKDNKGENPIDTAfkyinKDPVIKDIIANAVLIKEAD 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-348 1.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   65 ACSSGDTDEVKKLLARGADINTVNV-DGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYF 143
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  144 ISHGASVGIVNSEGEVPsdlaeepamkdlLLEQVKKQGVDLeqsrkeeeqqmlqdARQWLNSGRIEDVRQARSGATALHV 223
Cdd:PHA02875  155 IDHKACLDIEDCCGCTP------------LIIAMAKGDIAI--------------CKMLLDSGANIDYFGKNGCVAALCY 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  224 AAAKGYSEVLRLLIQAGYELNVqdhdgwtplhaaAHWGVKEACSILaEALCDMDIrnklgqTPFDVADEGLVEHLEMLQK 303
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNI------------MFMIEGEECTIL-DMICNMCT------NLESEAIDALIADIAIRIH 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 568909313  304 KQDVLRSEKETRNKlieSDLNSKfqSGLFKNKEKMLYEEEIPKSQ 348
Cdd:PHA02875  270 KKTIRRDEGFKNNM---STIEDK--EEFKDVFEKCIIELRRIKSE 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-150 3.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQA-CIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNI 139
Cdd:PHA02876  311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90
                  ....*....|.
gi 568909313  140 AEYFISHGASV 150
Cdd:PHA02876  391 INTLLDYGADI 401
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-305 3.65e-08

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: 57.33  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   45 LQTRRGSprvrfeDGAVFLAAcSSGDTDEVKKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANVNQ--- 119
Cdd:cd22192    11 LQQKRIS------ESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmt 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  120 -QDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqd 198
Cdd:cd22192    84 sDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY------------------------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  199 arqwlnsgriedvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD 277
Cdd:cd22192   135 -----------------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYD 196

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568909313  278 ----------IRNKLGQTPFDVA-DEGLVEHLEMLQKKQ 305
Cdd:cd22192   197 keddlqpldlVPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 542-810 7.01e-08

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 56.51  E-value: 7.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   542 TIAPSTYTSTYLKSASFGKSSDPTSPYISANRN-SSPATSPITIGSSTSRGSQwQPASSCPAPVSTNTPAPVQHVRTPYK 620
Cdd:pfam17823   64 TAAPAPVTLTKGTSAAHLNSTEVTAEHTPHGTDlSEPATREGAADGAASRALA-AAASSSPSSAAQSLPAAIAALPSEAF 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   621 SQADSTAEKTADSVSSSTPLCVI----TNRPAPSTANGVPAATVFSSAGTDPSVEAREKRRSYLTPVRD---------EE 687
Cdd:pfam17823  143 SAPRAAACRANASAAPRAAIAAAsaphAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGistaatatgHP 222

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   688 AESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSrSRAERQAQEQPGEKLEDPGGLEGSTKKQEPS-------AAPTKG 760
Cdd:pfam17823  223 AAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLA-AAAGTVASAAGTINMGDPHARRLSPAKHMPSdtmarnpAAPMGA 301

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568909313   761 AGEGRSLE---EEPIYHRLRYPTqPDKPTTPVSPSASRPSLYTGSHLLRTSRA 810
Cdd:pfam17823  302 QAQGPIIQvstDQPVHNTAGEPT-PSPSNTTLEPNTPKSVASTNLAVVTTTKA 353
PHA02798 PHA02798
ankyrin-like protein; Provisional
 71-157 1.32e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.61  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   71 TDEVKKLLARGADINTVNVDGLTALhqaC------IDEN--LDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAE- 141
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                          90
                  ....*....|....*...
gi 568909313  142 --YFISHGASVGIVNSEG 157
Cdd:PHA02798  128 llFMIENGADTTLLDKDG 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
203-257 2.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568909313   203 LNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-152 4.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLH-AAASCGYLNIAEYF 143
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLL 254


                  ....*....
gi 568909313  144 ISHGASVGI 152
Cdd:PHA02878  255 LEHGVDVNA 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-254 1.11e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   63 LAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEy 142
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR- 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  143 FISHGASVGIVNSEGEVPSDLAEE---PAMKDLLleqvkKQGVDLEQsrkeeeqqmlqdarqwlnsgriEDvrqaRSGAT 219
Cdd:PLN03192  609 ILYHFASISDPHAAGDLLCTAAKRndlTAMKELL-----KQGLNVDS----------------------ED----HQGAT 657

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568909313  220 ALHVAAAKGYSEVLRLLIQAGYELN-VQDHDGWTPL 254
Cdd:PLN03192  658 ALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT 693
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-122 1.22e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 1.22e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568909313    90 DGLTALHQACIDE-NLDMVKFLVENRANVNQQDN 122
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-118 5.71e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 5.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568909313   65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 935-1051 8.39e-06

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 47.59  E-value: 8.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   935 RDYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVE------KRERRALERKMSEMEEEM 1008
Cdd:pfam13851   43 ERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLEkelkdlKWEHEVLEQRFEKVERER 122

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 568909313  1009 KNLHQlKQIQTLKQMNEQLQAENRALTRVVARLSKSIESSDTQ 1051
Cdd:pfam13851  123 DELYD-KFEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQ 164
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-154 1.08e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.08e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568909313   123 EGWTPLHAAA-SCGYLNIAEYFISHGASVGIVN 154
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-150 1.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   60 AVFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDE-NLDMVKFLVENRANVNQQDNEGWTPLHAAasCGYLN 138
Cdd:PHA02876  411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                          90
                  ....*....|..
gi 568909313  139 IAEYFISHGASV 150
Cdd:PHA02876  489 IVNILLHYGAEL 500
DUF3432 pfam11914
Domain of unknown function (DUF3432); This presumed domain is functionally uncharacterized. ...
 576-659 1.72e-05

Domain of unknown function (DUF3432); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 100 amino acids in length. This domain is found associated with pfam00096. This domain has two conserved sequence motifs: YPSPV and PSP.


Pssm-ID: 403204 [Multi-domain]  Cd Length: 98  Bit Score: 44.71  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   576 SPATSPITIGSSTsrgsqwqPASSCPAPVSTNTPAPvqhVRTPYKSqadstaektadSVSSSTPLCVITNRPAPSTANGV 655
Cdd:pfam11914    6 ASAVSSISSYSSS-------VTTSYPSPITTSYPSP---VSTSYSS-----------PVPSSYPSPVHTSFPSPSIATTY 64


                   ....
gi 568909313   656 PAAT 659
Cdd:pfam11914   65 PSVT 68
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-117 4.90e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 4.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568909313   59 GAVFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANV 117
Cdd:PLN03192  623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-118 4.94e-05

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: 41.09  E-value: 4.94e-05
                           10        20
                   ....*....|....*....|....*....
gi 568909313    90 DGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 225-292 5.09e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909313  225 AAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 292
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-150 8.45e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 8.45e-05
                            10        20
                    ....*....|....*....|....*...
gi 568909313    123 EGWTPLHAAASCGYLNIAEYFISHGASV 150
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-302 9.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 9.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568909313   250 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGlvEHLEMLQ 302
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN--GNVEVLK 51
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-248 1.20e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.20e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568909313   217 GATALHVAAAK-GYSEVLRLLIQAGYELNVQDH 248
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 107-172 2.01e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909313  107 VKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDL 172
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-118 2.28e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.28e-04
                            10        20
                    ....*....|....*....|....*....
gi 568909313     90 DGLTALHQACIDENLDMVKFLVENRANVN 118
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 939-1048 2.54e-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: 44.75  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  939 KLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEktsdrssVLEVEKRERRALERKMSEMEEEMKNLHqlKQIQ 1018
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                          90       100       110
                  ....*....|....*....|....*....|
gi 568909313 1019 TLKQMNEQLQAENRALTRVVARLSKSIESS 1048
Cdd:COG4942   210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 215-304 2.77e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  215 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQDH-DGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 285
Cdd:PHA02736   53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                          90       100
                  ....*....|....*....|
gi 568909313  286 PFDVA-DEGLVEHLEMLQKK 304
Cdd:PHA02736  129 PYYVAcERHDAKMMNILRAK 148
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 72-163 3.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   72 DEVKKLLARGADINTVNVDGLTALHQAC--IDENLDMVKFLVENRANVNQQDNEGWTPLHAaascgYL------NIAEYF 143
Cdd:PHA02859  104 EILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                          90       100
                  ....*....|....*....|
gi 568909313  144 ISHGASVGIVNSEGEVPSDL 163
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDL 198
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 955-1046 4.89e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 44.17  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  955 LQEAQLELADIKAKLEKMAQQKQEktsdRSSVLEVEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA- 1033
Cdd:PRK11448  144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQk 217

                          90
                  ....*....|...
gi 568909313 1034 LTRVVARLSKSIE 1046
Cdd:PRK11448  218 RKEITDQAAKRLE 230
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 91-257 5.05e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   91 GLTALHQACIDENLDMVKFLVENRANVNQQDNE-------------GWTPLHAAASCGYLNIAEYFISHGASvgivnseg 157
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ-------- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  158 evPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQ---QMLQDARQWLNSGRIEDVRQaRSGATALHVAAAKGYSEVLR 234
Cdd:cd21882   145 --PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQmynLLLSYGAHLDPTQQLEEIPN-HQGLTPLKLAAVEGKIVMFQ 221

                         170       180
                  ....*....|....*....|....*....
gi 568909313  235 LLIQ----AGYELNVQDHDGWT--PLHAA 257
Cdd:cd21882   222 HILQrefsGPYQPLSRKFTEWTygPVTSS 250
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-160 9.30e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 9.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909313  101 DENLDMVKFLVENRANVNQQDNEGWTPLHAAASC-----GYLNIAEYFISHGASVGIVNSEGEVP 160
Cdd:PHA02798   48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP 112
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 1.00e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313    91 GLTALHQACIDENLDMVKFLVENRANVNQQDN--------------EGWTPLHAAASCGYLNIAEYFISHGASVGIVNSE 156
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   157 G-EVPSDLAEEPAMKDL---LLEQVKKQGVD-LEQSRKEEEqqmlqdarqwlnsgrIEDVRQaRSGATALHVAAAKGYSE 231
Cdd:TIGR00870  208 GnTLLHLLVMENEFKAEyeeLSCQMYNFALSlLDKLRDSKE---------------LEVILN-HQGLTPLKLAAKEGRIV 271

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568909313   232 VLRLLIQAGYElnVQDHDGWT--PLHAAAHW 260
Cdd:TIGR00870  272 LFRLKLAIKYK--QKKFVAWPngQQLLSLYW 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 217-245 1.08e-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: 37.18  E-value: 1.08e-03
                            10        20
                    ....*....|....*....|....*....
gi 568909313    217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 509-796 1.28e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  509 EKENRESAVNLVRSGSHTRQLWRdEAKGSETPQTIAPSTYTSTYLKSASFGKSSDPTSPYISANRNSSPATsPITIGSST 588
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGR-AAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSAT-PLPPGPAA 2727

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  589 SRGSQ-WQPASSCPAPVSTNTPAPVQhVRTPYKSQADSTAEKTA------------------DSVSSSTPLCVITNRPAP 649
Cdd:PHA03247 2728 ARQASpALPAAPAPPAVPAGPATPGG-PARPARPPTTAGPPAPAppaapaagpprrltrpavASLSESRESLPSPWDPAD 2806

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  650 STANGVPAA----TVFSSAGTDPSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 725
Cdd:PHA03247 2807 PPAAVLAPAaalpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568909313  726 AERQAQEQPGEKLEDPGGLEGSTKKQEPSAAPTKGAGEGRSLEEEPiyhrLRYPTQPDKPTTPVSPSASRP 796
Cdd:PHA03247 2887 ARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----PPPPPRPQPPLAPTTDPAGAG 2953
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 938-1025 1.52e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 39.97  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   938 KKLYESALTENQKLKTKLQEAQLELADI---KAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEMKNLHQL 1014
Cdd:pfam10473   51 KAEVETLKAEIEEMAQNLRDLELDLVTLrseKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEM 130

                           90
                   ....*....|.
gi 568909313  1015 KQIQtLKQMNE 1025
Cdd:pfam10473  131 LQTQ-LKELNE 140
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-290 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   94 ALHQACIDENLDMVKFLVENRANVNQQDNEGWTPLHAAASCGYLNIAEYFISHGAsvgivnsegeVPSdlAEEPAMKDLL 173
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------IPD--VKYPDIESEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  174 LEQVKKQGVdleqsRKEEEqqmlqdarqWLNSGRIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTP 253
Cdd:PHA02875   73 HDAVEEGDV-----KAVEE---------LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568909313  254 LHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 70-254 1.81e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.21  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   70 DTDEVKKLLARGADINTVNVDGLTALHQACIDENL--DMVKFLVENRANVNQQDNEGWTPLHAAASCG------------ 135
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  136 --YLNIAEYFISHGASVGIVNSEGEVP-------------SDLAeEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQ--- 197
Cdd:PHA02716  376 diRLDVIQCLISLGADITAVNCLGYTPltsyictaqnymyYDII-DCLISDKVLNMVKHRILQDLLIRVDDTPCIIHhii 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  198 -----------DARQWLNSGRIEDVRQAR------------SGATALHVAA-----AKGYSEVLRLLIQAGYELNVQDHD 249
Cdd:PHA02716  455 akyniptdlytDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKN 534


                  ....*
gi 568909313  250 GWTPL 254
Cdd:PHA02716  535 GVTPL 539
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 1.91e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.91e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909313   123 EGWTPLHAAASCGYLNIAEYFISHGASVGI 152
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 72-156 1.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   72 DEVKKLLARGADINTVNVDGLTA----LHQACIDeNLDMVKFLVENRANVNQQDNEGWTPLHAAASCGY---LNIAEYFI 144
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168

                          90
                  ....*....|..
gi 568909313  145 SHGASVGIVNSE 156
Cdd:PHA02798  169 EKGVDINTHNNK 180
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-98 2.35e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568909313    48 RRGSPRVRFEDGAVFLA---ACSSGDTDEVKKLLARGADINTVNVDGLTALHQA 98
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPlhvAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 74-129 2.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 2.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   74 VKKLLARGADIN-TVNVDGLTALHQ-ACIDENL--DMVKFLVENRANVNQQDNEGWTPLH 129
Cdd:PHA02859   69 LKFLIENGADVNfKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLH 128
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 514-829 2.64e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  514 ESAVNLVRSGSHTRQLWRDEAKGSET----PQTIAPSTYTSTYLKSASFGKSSDPTSPyisanrnssPATSPITIGSSTS 589
Cdd:PHA03307   52 AVTVVAGAAACDRFEPPTGPPPGPGTeapaNESRSTPTWSLSTLAPASPAREGSPTPP---------GPSSPDPPPPTPP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  590 RGSqwqPASSCPAPVSTNTPAPVQHVRTPYKSQADSTAEKTADSVSSSTPLcvitnRPAPSTANGVPAATVFSSAGTDPS 669
Cdd:PHA03307  123 PAS---PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSR-----QAALPLSSPEETARAPSSPPAEPP 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  670 VEAREKRRSYLTPVRDEEAESlrKARSRQARQTRRSTQGvtltdlqeAEKTFSRSRAERQAQEQPGEKLEDPGGLEGstk 749
Cdd:PHA03307  195 PSTPPAAASPRPPRRSSPISA--SASSPAPAPGRSAADD--------AGASSSDSSSSESSGCGWGPENECPLPRPA--- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  750 kqePSAAPTKGAGEGRSLEEEPIYHRLRYPTQPDKPTTPVSPSASRPSLYTGSHllRTSRASGPDSENSETSTHATAAKE 829
Cdd:PHA03307  262 ---PITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSP--RASSSSSSSRESSSSSTSSSSESS 336
fliH PRK06669
flagellar assembly protein H; Validated
 930-1051 2.84e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.77  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  930 EEDSNRDYKKLYESALTE-NQKLKTKLQEAQLELADIKAKLEKMAQQKQEktsdrssvlEVEKRERRALERKMSEMEEEM 1008
Cdd:PRK06669   50 REEANDEAKEIIEEAEEDaFEIVEAAEEEAKEELLKKTDEASSIIEKLQM---------QIEREQEEWEEELERLIEEAK 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568909313 1009 KNLHQLKQIQTLKQMNEQLQAENRALTRVVARLSKS----IESSDTQ 1051
Cdd:PRK06669  121 AEGYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKKreeiLESSEEE 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 3.32e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGRIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 568909313  233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-285 4.51e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  186 QSRKEEEQQMLQDARQW---LNSGRIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 255
Cdd:PLN03192  484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                          90       100       110
                  ....*....|....*....|....*....|
gi 568909313  256 AAAHWGVKEACSILAEALCDMDIRNKLGQT 285
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-281 4.73e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568909313   249 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 281
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
942-1051 5.31e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313  942 ESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDrssvLEVEKRERRALERKMSEMEEEMKNLHQlkQIQTLK 1021
Cdd:COG4372    48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ----LQAAQAELAQAQEELESLQEEAEELQE--ELEELQ 121

                          90       100       110
                  ....*....|....*....|....*....|
gi 568909313 1022 QMNEQLQAENRALTRVVARLSKSIESSDTQ 1051
Cdd:COG4372   122 KERQDLEQQRKQLEAQIAELQSEIAEREEE 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-245 5.51e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 5.51e-03
                           10        20
                   ....*....|....*....|....*....
gi 568909313   217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 931-1041 5.97e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.28  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   931 EDSNRDYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKM--------AQQKQEKTSDRSSVLE-VEKRERraLERKM 1001
Cdd:pfam04012   96 EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkarlkaakAQEAVQTSLGSLSTSSaTDSFER--IEEKI 173

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 568909313  1002 SEMEEEMKNLHQLKQIQTLKQMNEQLQAENRALTRVVARL 1041
Cdd:pfam04012  174 EEREARADAAAELASAVDLDAKLEQAGIQMEVSEDVLARL 213
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 68-160 6.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   68 SGDTDEVKKLLARGADINTVNVdglTALHqACIDE---NLDMVKFLVENRANVN-QQDNEGWTPLHAaascgYLN----- 138
Cdd:PHA02859   31 KDDIEGVKKWIKFVNDCNDLYE---TPIF-SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHH-----YLSfnknv 101

                          90       100
                  ....*....|....*....|....*
gi 568909313  139 ---IAEYFISHGASVGIVNSEGEVP 160
Cdd:PHA02859  102 epeILKILIDSGSSITEEDEDGKNL 126
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 942-1044 7.24e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.37  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   942 ESALTENQKLKTKLQEaqleladIKAKLEKMAQQKQEktsdrssvlevEKRERRALERKMSEMEEEMKnlhqlKQIQTLK 1021
Cdd:pfam09744   39 ESLASRNQEHNVELEE-------LREDNEQLETQYER-----------EKALRKRAEEELEEIEDQWE-----QETKDLL 95

                           90       100
                   ....*....|....*....|....
gi 568909313  1022 QMNEQLQAENRAL-TRVVARLSKS 1044
Cdd:pfam09744   96 SQVESLEEENRRLeADHVSRLEEK 119
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 72-164 9.40e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.13  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   72 DEVKKLLARGADIN----------TVNVDGL----TALHQACIDENLDMVKFLVEN-RANVNQQDNEGWTPLHAaascgY 136
Cdd:cd22194   155 DIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEIVQLLMEKeSTDITSQDSRGNTVLHA-----L 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568909313  137 LNIAEYFISHGASV-----------------GIVNSEGEVPSDLA 164
Cdd:cd22194   230 VTVAEDSKTQNDFVkrmydmillksenknleTIRNNEGLTPLQLA 274
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 946-1050 9.63e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909313   946 TENQKLKTKLQEAQLELADIK----AKLEKMAQQKQEKTSDRSSVLEVEKRERralerkmsEMEEEMKNLHQ-----LKQ 1016
Cdd:TIGR04523  356 SENSEKQRELEEKQNEIEKLKkenqSYKQEIKNLESQINDLESKIQNQEKLNQ--------QKDEQIKKLQQekellEKE 427

                           90       100       110
                   ....*....|....*....|....*....|....
gi 568909313  1017 IQTLKQMNEQLQAENRALTRVVARLSKSIESSDT 1050
Cdd:TIGR04523  428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
 
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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