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Conserved domains on  [gi|1958672379|ref|XP_038946648|]
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protein phosphatase 1 regulatory subunit 12B isoform X7 [Rattus norvegicus]

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 1.24e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672379 222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 606-662 3.04e-20

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: 84.96  E-value: 3.04e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 606 ASVEPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 662
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
PHA03369 super family cl25753
capsid maturational protease; Provisional
 499-786 2.49e-03

capsid maturational protease; Provisional


The actual alignment was detected with superfamily member PHA03369:

Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 41.52  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 499 RRLSGTSDIEEKENRESAVNLVRSGSHTRQLWRDEAKGNETPQTVAPSTYTSTYLKRTPYKSQADSTAERTDSGSS---- 574
Cdd:PHA03369  326 QYLIEGRKLFSTINGLKAHNEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTaypp 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 575 -----STPLCVITNRPAPSTaNGVPAATVLSSPAAdaSVEPREQRRSYLTPVRDEEAeslrkarSRQARQTRRSTQGVTL 649
Cdd:PHA03369  406 vpqfcGDPGLVSPYNPQSPG-TSYGPEPVGPVPPQ--PTNPYVMPISMANMVYPGHP-------QEHGHERKRKRGGELK 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 650 TDLQEAEKTFSRSRAERQAQEQPGEKLEDSGELEgSTKKQEPSAAPTKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDklt 729
Cdd:PHA03369  476 EELIETLKLVKKLKEEQESLAKELEATAHKSEIK-KIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPETKTE--- 551

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 730 apvspSASRPSLYTGSQLLHTSRASVPDPEATTNTTAAKEMDTSEKEEADLDDQSSN 786
Cdd:PHA03369  552 -----LEAVVRFPYQIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAIETLLTQ 603
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 169-257 2.82e-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: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 1958672379 233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-290 1.24e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672379 222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.85e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 97.88  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANINQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1958672379 145 SHGASVGIVN 154
Cdd:pfam12796  82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 606-662 3.04e-20

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: 84.96  E-value: 3.04e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 606 ASVEPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 662
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 2.33e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANINQQDNEGWTPLHAAAS------ 133
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfninp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 134 ------------------CGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKkqgvdleQSRKEEEQQM 195
Cdd:PHA03095  133 kvirlllrkgadvnaldlYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHL-------QSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 196 lqdaRQWLNSGKIEDVRQaRSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEAL 273
Cdd:PHA03095  206 ----RELIRAGCDPAATD-MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 1958672379 274 CDMDIRNKLGQTPFDVA 290
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-305 2.75e-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: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  45 LQTRRGSprvrfeDGAVFLAAcSSGDTDEVKKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANINQ--- 119
Cdd:cd22192    11 LQQKRIS------ESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmt 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 120 -QDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqd 198
Cdd:cd22192    84 sDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY------------------------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 199 arqwlnsgkiedvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD 277
Cdd:cd22192   135 -----------------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYD 196

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958672379 278 ----------IRNKLGQTPFDVA-DEGLVEHLEMLQKKQ 305
Cdd:cd22192   197 keddlqpldlVPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-150 6.87e-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: 6.87e-05
                           10        20
                   ....*....|....*....|....*...
gi 1958672379  123 EGWTPLHAAASCGYLNIAEYFISHGASV 150
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 6.50e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  91 GLTALHQACIDENLDMVKFLVENRANINQQDN--------------EGWTPLHAAASCGYLNIAEYFISHGASVGIVNSE 156
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 157 G-EVPSDLAEEPAMKDLLLEqvkkqgvdLEQSRKEEEQQMLQDARqwlNSGKIEDVRQaRSGATALHVAAAKGYSEVLRL 235
Cdd:TIGR00870 208 GnTLLHLLVMENEFKAEYEE--------LSCQMYNFALSLLDKLR---DSKELEVILN-HQGLTPLKLAAKEGRIVLFRL 275

                         170       180
                  ....*....|....*....|....*..
gi 1958672379 236 LIQAGYElnVQDHDGWT--PLHAAAHW 260
Cdd:TIGR00870 276 KLAIKYK--QKKFVAWPngQQLLSLYW 300
PHA03369 PHA03369
capsid maturational protease; Provisional
 499-786 2.49e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 41.52  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 499 RRLSGTSDIEEKENRESAVNLVRSGSHTRQLWRDEAKGNETPQTVAPSTYTSTYLKRTPYKSQADSTAERTDSGSS---- 574
Cdd:PHA03369  326 QYLIEGRKLFSTINGLKAHNEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTaypp 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 575 -----STPLCVITNRPAPSTaNGVPAATVLSSPAAdaSVEPREQRRSYLTPVRDEEAeslrkarSRQARQTRRSTQGVTL 649
Cdd:PHA03369  406 vpqfcGDPGLVSPYNPQSPG-TSYGPEPVGPVPPQ--PTNPYVMPISMANMVYPGHP-------QEHGHERKRKRGGELK 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 650 TDLQEAEKTFSRSRAERQAQEQPGEKLEDSGELEgSTKKQEPSAAPTKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDklt 729
Cdd:PHA03369  476 EELIETLKLVKKLKEEQESLAKELEATAHKSEIK-KIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPETKTE--- 551

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 730 apvspSASRPSLYTGSQLLHTSRASVPDPEATTNTTAAKEMDTSEKEEADLDDQSSN 786
Cdd:PHA03369  552 -----LEAVVRFPYQIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAIETLLTQ 603
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 2.82e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 1958672379 233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-290 1.24e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666   171 LLLEAGADVNARDNDGE------------------------------------------------------------TPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672379 222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-305 4.82e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 4.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAE 141
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 142 YFISHGASVGIVNSEGEvpsdlaeepamkdllleqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkiedvrqarsgaTAL 221
Cdd:COG0666   138 LLLEAGADVNAQDNDGN------------------------------------------------------------TPL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 222 HVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-DEGLVEHLEM 300
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaENGNLEIVKL 237


                  ....*
gi 1958672379 301 LQKKQ 305
Cdd:COG0666   238 LLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-215 1.11e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  63 LAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEY 142
Cdd:COG0666   125 HLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958672379 143 FISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQDARQWLNSGKIEDVRQAR 215
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-154 1.85e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 97.88  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENrANINQQDNeGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1958672379 145 SHGASVGIVN 154
Cdd:pfam12796  82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 606-662 3.04e-20

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: 84.96  E-value: 3.04e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 606 ASVEPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 662
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 609-661 3.15e-20

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: 84.75  E-value: 3.15e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958672379 609 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 661
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 61-290 2.33e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALH-QACIDENLDMVKFLVENRANINQQDNEGWTPLHAAAS------ 133
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfninp 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 134 ------------------CGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKkqgvdleQSRKEEEQQM 195
Cdd:PHA03095  133 kvirlllrkgadvnaldlYGMTPLAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHL-------QSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 196 lqdaRQWLNSGKIEDVRQaRSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEAL 273
Cdd:PHA03095  206 ----RELIRAGCDPAATD-MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         250
                  ....*....|....*..
gi 1958672379 274 CDMDIRNKLGQTPFDVA 290
Cdd:PHA03095  281 ADINAVSSDGNTPLSLM 297
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 611-663 2.35e-19

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: 82.40  E-value: 2.35e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958672379 611 REQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 663
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-247 1.61e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  95 LHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGasvgivnsegevpsdlaeepamkdlll 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958672379 175 eqvkkqgvdleqsrkeeeqqmlqdarqwlnsgkieDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 247
Cdd:pfam12796  54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-258 2.24e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.57  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  72 DEVKKLLARGADINTVNVDGLTALH-----QACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASC--GYLNIAEYFI 144
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 145 SHGASVGIVNSEGEVPSDLAEEPAMKDL-LLEQVKKQGVDLEQSRKEEeqqMLqdarqwLNSGKIEDVRQARsGATALHV 223
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKIDLkILKLLIDKGVDINAKNRVN---YL------LSYGVPINIKDVY-GFTPLHY 198

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958672379 224 AAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAA 258
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 611-657 2.42e-18

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: 78.92  E-value: 2.42e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958672379 611 REQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEK 657
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-164 6.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 6.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  62 FLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQA--CIDENLDMVKFLVENRANINQQ----------------DNE 123
Cdd:PHA03100  112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVY 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958672379 124 GWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-144 8.34e-16

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 71.92  E-value: 8.34e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958672379  91 GLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFI 144
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-301 2.21e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 221 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 299
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 1958672379 300 ML 301
Cdd:pfam12796  79 LL 80
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 609-658 7.54e-15

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: 69.52  E-value: 7.54e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958672379 609 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKT 658
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 70-290 1.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  70 DTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGAS 149
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 150 VGIVNSEGEVPSDLAEE---PAMKDLLLEqvkkqgvdleqsrkeeeqqmlqdarqwlNSGKIEDvrQARSGATALHVAAA 226
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEygdYACIKLLID----------------------------HGNHIMN--KCKNGFTPLHNAII 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672379 227 KGYSeVLRLLIQaGYELNVQDHDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02874  233 HNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-290 1.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDnegwTPLHAAASCGYLNIAEYFI 144
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 145 SHGASVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDleqsrkeeeqqmlqdarqwLNSGKIEdvrqarsGATALHVA 224
Cdd:PHA02876  261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGAD-------------------VNAKNIK-------GETPLYLM 314

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672379 225 AAKGY-SEVLRLLIQAGYELNVQDHDGWTPLHAAAHWG-VKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02876  315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA 382
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-290 2.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  85 NTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 165 EEPA--MKDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQA 239
Cdd:PHA02878  111 NRNVeiFKIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSY 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958672379 240 GYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 72-155 2.66e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 2.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  72 DEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGASVG 151
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ....
gi 1958672379 152 IVNS 155
Cdd:PHA03100  253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-269 5.32e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958672379 219 TALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSIL 269
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 2.43e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.59  E-value: 2.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672379  77 LLARG-ADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-121 2.72e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 2.72e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672379  64 AACSSGDTDEVkKLLARGADINtVNVDGLTALHQACIDENLDMVKFLVENRANINQQD 121
Cdd:pfam12796  36 LAAKNGHLEIV-KLLLEHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 70-283 2.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  70 DTDEVKKLLARGADINTVNVDGL-TALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGA 148
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 149 SVGIVNSEGEVPSDLAEEPAMKDLLLEQVKKQGVDLeqsrkeeeqqmlqdarqwlnsgkieDVRQARSGATALHVAAAKg 228
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV-------------------------NAKSYILGLTALHSSIKS- 279

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958672379 229 ySEVLRLLIQAGYELNVQDHDGWTPLHAAA--HWGVkEACSILAEALC-----DMDIRNKLG 283
Cdd:PHA02878  280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCI-NIGRILISNICllkriKPDIKNSEG 339
Ank_4 pfam13637
Ankyrin repeats (many copies);
61-111 6.77e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 6.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958672379  61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLV 111
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-292 2.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 103 NLDMVKFLVENRAN-INQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEgeVPSDL------AEEPAMKDLLLE 175
Cdd:PHA02874   13 DIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK--IPHPLltaikiGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 176 QVKKQGVDLEQSRKEEEQQMLQdarqwlnSGKIEDVRQARSgATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 255
Cdd:PHA02874   91 GVDTSILPIPCIEKDMIKTILD-------CGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958672379 256 AAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 292
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 69-183 4.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 4.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  69 GDTDEVKKLLARGADINTVNVDGLTALHQACIdENLDMVKFLVENRAnINQQDNEGWTPLHAAAS--CGyLNIAEYFISH 146
Cdd:PHA02874  201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLINNAS-INDQDIDGSTPLHHAINppCD-IDIIDILLYH 277

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958672379 147 GASVGIVNSEGEVPSDLA-----EEPAMKDLLLEQVKKQGVD 183
Cdd:PHA02874  278 KADISIKDNKGENPIDTAfkyinKDPVIKDIIANAVLIKEAD 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-159 5.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  54 VRFEDGAVFL-AACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAA 132
Cdd:PHA02875   97 VFYKDGMTPLhLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                          90       100
                  ....*....|....*....|....*..
gi 1958672379 133 SCGYLNIAEYFISHGASVGIVNSEGEV 159
Cdd:PHA02875  177 AKGDIAICKMLLDSGANIDYFGKNGCV 203
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 8.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 8.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672379 110 LVENR-ANINQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-348 1.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNV-DGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYF 143
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 144 ISHGASVGIVNSEGEVPsdlaeepamkdlLLEQVKKQGVDLeqsrkeeeqqmlqdARQWLNSGKIEDVRQARSGATALHV 223
Cdd:PHA02875  155 IDHKACLDIEDCCGCTP------------LIIAMAKGDIAI--------------CKMLLDSGANIDYFGKNGCVAALCY 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 224 AAAKGYSEVLRLLIQAGYELNVqdhdgwtplhaaAHWGVKEACSILaEALCDMDIrnklgqTPFDVADEGLVEHLEMLQK 303
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGADCNI------------MFMIEGEECTIL-DMICNMCT------NLESEAIDALIADIAIRIH 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958672379 304 KQDVLRSEKETRNKlieSDLNSKfqSGLFKNKEKMLYEEEIPKSQ 348
Cdd:PHA02875  270 KKTIRRDEGFKNNM---STIEDK--EEFKDVFEKCIIELRRIKSE 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 63-169 1.38e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  63 LAAcsSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEY 142
Cdd:PTZ00322   89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958672379 143 FISH------GASVGIVNSEGEVPSDLAEEPAM 169
Cdd:PTZ00322  167 LSRHsqchfeLGANAKPDSFTGKPPSLEDSPIS 199
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-305 2.75e-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: 2.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  45 LQTRRGSprvrfeDGAVFLAAcSSGDTDEVKKLL-ARGADINTVNVDGLTALHQACIDENLDMVKFLVEN-RANINQ--- 119
Cdd:cd22192    11 LQQKRIS------ESPLLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAaPELVNEpmt 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 120 -QDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSdlaeePAMKDLLLeqvkkqgvdleqsrkeeeqqmlqd 198
Cdd:cd22192    84 sDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFFR-----PGPKNLIY------------------------ 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 199 arqwlnsgkiedvrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD 277
Cdd:cd22192   135 -----------------YGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYD 196

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958672379 278 ----------IRNKLGQTPFDVA-DEGLVEHLEMLQKKQ 305
Cdd:cd22192   197 keddlqpldlVPNNQGLTPFKLAaKEGNIVMFQHLVQKR 235
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-150 4.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  61 VFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQA-CIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNI 139
Cdd:PHA02876  311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90
                  ....*....|.
gi 1958672379 140 AEYFISHGASV 150
Cdd:PHA02876  391 INTLLDYGADI 401
PHA02798 PHA02798
ankyrin-like protein; Provisional
 71-157 7.81e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.61  E-value: 7.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  71 TDEVKKLLARGADINTVNVDGLTALhqaC------IDEN--LDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAE- 141
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                          90
                  ....*....|....*...
gi 1958672379 142 --YFISHGASVGIVNSEG 157
Cdd:PHA02798  128 llFMIENGADTTLLDKDG 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
203-257 1.57e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.57e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958672379 203 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-152 1.81e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLH-AAASCGYLNIAEYF 143
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLL 254


                  ....*....
gi 1958672379 144 ISHGASVGI 152
Cdd:PHA02878  255 LEHGVDVNA 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-254 9.60e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 9.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  63 LAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEy 142
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR- 608

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 143 FISHGASVGIVNSEGEVPSDLAEE---PAMKDLLleqvkKQGVDLEQsrkeeeqqmlqdarqwlnsgkiEDvrqaRSGAT 219
Cdd:PLN03192  609 ILYHFASISDPHAAGDLLCTAAKRndlTAMKELL-----KQGLNVDS----------------------ED----HQGAT 657

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958672379 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: 45.36  E-value: 1.22e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958672379  90 DGLTALHQACIDE-NLDMVKFLVENRANINQQDN 122
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-118 1.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 1.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958672379  65 ACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANIN 118
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-154 8.77e-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: 43.05  E-value: 8.77e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958672379 123 EGWTPLHAAA-SCGYLNIAEYFISHGASVGIVN 154
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-150 1.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  60 AVFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDE-NLDMVKFLVENRANINQQDNEGWTPLHAAasCGYLN 138
Cdd:PHA02876  411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                          90
                  ....*....|..
gi 1958672379 139 IAEYFISHGASV 150
Cdd:PHA02876  489 IVNILLHYGAEL 500
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 90-118 2.29e-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: 41.86  E-value: 2.29e-05
                          10        20
                  ....*....|....*....|....*....
gi 1958672379  90 DGLTALHQACIDENLDMVKFLVENRANIN 118
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 225-292 3.34e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958672379 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 6.87e-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: 6.87e-05
                           10        20
                   ....*....|....*....|....*...
gi 1958672379  123 EGWTPLHAAASCGYLNIAEYFISHGASV 150
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-302 7.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 7.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958672379 250 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGlvEHLEMLQ 302
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN--GNVEVLK 51
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 59-117 8.80e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 8.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958672379  59 GAVFLAACSSGDTDEVKKLLARGADINTVNVDGLTALHQACIDENLDMVKFLVENRANI 117
Cdd:PLN03192  623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-248 9.71e-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: 40.35  E-value: 9.71e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958672379 217 GATALHVAAAK-GYSEVLRLLIQAGYELNVQDH 248
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 90-118 1.01e-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: 39.88  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958672379   90 DGLTALHQACIDENLDMVKFLVENRANIN 118
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 72-163 1.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  72 DEVKKLLARGADINTVNVDGLTALHQAC--IDENLDMVKFLVENRANINQQDNEGWTPLHAaascgYL------NIAEYF 143
Cdd:PHA02859  104 EILKILIDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                          90       100
                  ....*....|....*....|
gi 1958672379 144 ISHGASVGIVNSEGEVPSDL 163
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDL 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 107-172 1.54e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958672379 107 VKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGASVGIVNSEGEVPSDLAEEPAMKDL 172
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 215-304 2.20e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 215 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQDH-DGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 285
Cdd:PHA02736   53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                          90       100
                  ....*....|....*....|
gi 1958672379 286 PFDVA-DEGLVEHLEMLQKK 304
Cdd:PHA02736  129 PYYVAcERHDAKMMNILRAK 148
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 91-257 4.39e-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: 43.72  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  91 GLTALHQACIDENLDMVKFLVENRANINQQDNE-------------GWTPLHAAASCGYLNIAEYFISHGASvgivnseg 157
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ-------- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 158 evPSDLAEEPAMKDLLLEQVKKQGVDLEQSRKEEEQ---QMLQDARQWLNSGKIEDVRQaRSGATALHVAAAKGYSEVLR 234
Cdd:cd21882   145 --PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQmynLLLSYGAHLDPTQQLEEIPN-HQGLTPLKLAAVEGKIVMFQ 221

                         170       180
                  ....*....|....*....|....*....
gi 1958672379 235 LLIQ----AGYELNVQDHDGWT--PLHAA 257
Cdd:cd21882   222 HILQrefsGPYQPLSRKFTEWTygPVTSS 250
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 70-254 5.64e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 43.75  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  70 DTDEVKKLLARGADINTVNVDGLTALHQACIDENL--DMVKFLVENRANINQQDNEGWTPLHAAASCG------------ 135
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 136 --YLNIAEYFISHGASVGIVNSEGEVP-------------SDLAeEPAMKDLLLEQVKKQGVDLEQSRKEEEQQMLQ--- 197
Cdd:PHA02716  376 diRLDVIQCLISLGADITAVNCLGYTPltsyictaqnymyYDII-DCLISDKVLNMVKHRILQDLLIRVDDTPCIIHhii 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 198 -----------DARQWLNSGKIEDVRQAR------------SGATALHVAA-----AKGYSEVLRLLIQAGYELNVQDHD 249
Cdd:PHA02716  455 akyniptdlytDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKN 534


                  ....*
gi 1958672379 250 GWTPL 254
Cdd:PHA02716  535 GVTPL 539
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-290 5.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  94 ALHQACIDENLDMVKFLVENRANINQQDNEGWTPLHAAASCGYLNIAEYFISHGAsvgivnsegeVPSdlAEEPAMKDLL 173
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------IPD--VKYPDIESEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 174 LEQVKKQGVdleqsRKEEEqqmlqdarqWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTP 253
Cdd:PHA02875   73 HDAVEEGDV-----KAVEE---------LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958672379 254 LHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 290
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 91-260 6.50e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  91 GLTALHQACIDENLDMVKFLVENRANINQQDN--------------EGWTPLHAAASCGYLNIAEYFISHGASVGIVNSE 156
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 157 G-EVPSDLAEEPAMKDLLLEqvkkqgvdLEQSRKEEEQQMLQDARqwlNSGKIEDVRQaRSGATALHVAAAKGYSEVLRL 235
Cdd:TIGR00870 208 GnTLLHLLVMENEFKAEYEE--------LSCQMYNFALSLLDKLR---DSKELEVILN-HQGLTPLKLAAKEGRIVLFRL 275

                         170       180
                  ....*....|....*....|....*..
gi 1958672379 236 LIQAGYElnVQDHDGWT--PLHAAAHW 260
Cdd:TIGR00870 276 KLAIKYK--QKKFVAWPngQQLLSLYW 300
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 217-245 8.74e-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: 37.18  E-value: 8.74e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958672379  217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 74-129 1.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  74 VKKLLARGADIN-TVNVDGLTALHQ-ACIDENL--DMVKFLVENRANINQQDNEGWTPLH 129
Cdd:PHA02859   69 LKFLIENGADVNfKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLH 128
PHA02798 PHA02798
ankyrin-like protein; Provisional
 72-156 1.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  72 DEVKKLLARGADINTVNVDGLTA----LHQACIDeNLDMVKFLVENRANINQQDNEGWTPLHAAASCGY---LNIAEYFI 144
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168

                          90
                  ....*....|..
gi 1958672379 145 SHGASVGIVNSE 156
Cdd:PHA02798  169 EKGVDINTHNNK 180
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-160 1.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958672379 101 DENLDMVKFLVENRANINQQDNEGWTPLHAAASC-----GYLNIAEYFISHGASVGIVNSEGEVP 160
Cdd:PHA02798   48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP 112
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-285 1.53e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 186 QSRKEEEQQMLQDARQW---LNSGKIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 255
Cdd:PLN03192  484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958672379 256 AAAHWGVKEACSILAEALCDMDIRNKLGQT 285
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 1.55e-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: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958672379 123 EGWTPLHAAASCGYLNIAEYFISHGASVGI 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
48-98 1.90e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958672379  48 RRGSPRVRFEDGAVFLA---ACSSGDTDEVKKLLARGADINTVNVDGLTALHQA 98
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPlhvAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03369 PHA03369
capsid maturational protease; Provisional
 499-786 2.49e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 41.52  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 499 RRLSGTSDIEEKENRESAVNLVRSGSHTRQLWRDEAKGNETPQTVAPSTYTSTYLKRTPYKSQADSTAERTDSGSS---- 574
Cdd:PHA03369  326 QYLIEGRKLFSTINGLKAHNEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTaypp 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 575 -----STPLCVITNRPAPSTaNGVPAATVLSSPAAdaSVEPREQRRSYLTPVRDEEAeslrkarSRQARQTRRSTQGVTL 649
Cdd:PHA03369  406 vpqfcGDPGLVSPYNPQSPG-TSYGPEPVGPVPPQ--PTNPYVMPISMANMVYPGHP-------QEHGHERKRKRGGELK 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 650 TDLQEAEKTFSRSRAERQAQEQPGEKLEDSGELEgSTKKQEPSAAPTKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDklt 729
Cdd:PHA03369  476 EELIETLKLVKKLKEEQESLAKELEATAHKSEIK-KIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPETKTE--- 551

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958672379 730 apvspSASRPSLYTGSQLLHTSRASVPDPEATTNTTAAKEMDTSEKEEADLDDQSSN 786
Cdd:PHA03369  552 -----LEAVVRFPYQIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAIETLLTQ 603
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 169-257 2.82e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 169 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 232
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 1958672379 233 LRLLIQAGYELNVQDHDGWTPLHAA 257
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-281 3.84e-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: 3.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958672379 249 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 281
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 217-245 4.48e-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: 4.48e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958672379 217 GATALHVAAAKGYSEVLRLLIQAGYELNV 245
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 72-164 5.26e-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: 40.51  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  72 DEVKKLLARGADIN----------TVNVDGL----TALHQACIDENLDMVKFLVEN-RANINQQDNEGWTPLHAaascgY 136
Cdd:cd22194   155 DIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEIVQLLMEKeSTDITSQDSRGNTVLHA-----L 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958672379 137 LNIAEYFISHGASV-----------------GIVNSEGEVPSDLA 164
Cdd:cd22194   230 VTVAEDSKTQNDFVkrmydmillksenknleTIRNNEGLTPLQLA 274
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
543-744 5.37e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 543 VAPSTY---TSTYLKRTPYKSQADSTAERTDSGSSSTPLCVITNRPAPSTANGVPAATVLSSPAADASVEPREQRRSYLT 619
Cdd:PRK07003  340 LAPDEYagfTMTLLRMLAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379 620 PVRdEEAESLRKARSRQA-RQTRRSTQGVTLTDLQEAEKTFSRSRAERQAQE--QPGEKLEDSGELEGSTKKQ-EPSAAP 695
Cdd:PRK07003  420 ATR-AEAPPAAPAPPATAdRGDDAADGDAPVPAKANARASADSRCDERDAQPpaDSGSASAPASDAPPDAAFEpAPRAAA 498

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958672379 696 TKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDKLTAPVSPSASRPSLYTG 744
Cdd:PRK07003  499 PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAG 547
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 68-160 6.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958672379  68 SGDTDEVKKLLARGADINTVNVdglTALHqACIDE---NLDMVKFLVENRANIN-QQDNEGWTPLHAaascgYLN----- 138
Cdd:PHA02859   31 KDDIEGVKKWIKFVNDCNDLYE---TPIF-SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHH-----YLSfnknv 101

                          90       100
                  ....*....|....*....|....*
gi 1958672379 139 ---IAEYFISHGASVGIVNSEGEVP 160
Cdd:PHA02859  102 epeILKILIDSGSSITEEDEDGKNL 126
 
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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