NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1578915130|ref|NP_001355665|]
View 

protein phosphatase 1 regulatory subunit 12A isoform 1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 930-1029 2.29e-43

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: 152.46  E-value: 2.29e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  930 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRSQL-EMEKRERRALERRISEMEEELKMLPDLK 1007
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLlETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 1578915130 1008 ADNQRLKDENGALIRVISKLSK 1029
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-331 8.32e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666     53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  119 LDIAEFLIGQGAHVGAVNSEGDTPldiaeeeameellqnevnrqgvdieaarkeeervmlrdarqwlnsghisdvrhaks 198
Cdd:COG0666    133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  199 ggtaLHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILG 278
Cdd:COG0666    157 ----LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  279 YLEELQKKQTLLHSEKRDKKSPLIESTANMENNQPQKAFKNKETLIIEPEKNA 331
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-712 1.64e-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: 83.03  E-value: 1.64e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  658 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 712
Cdd:cd21944      3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 930-1029 2.29e-43

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: 152.46  E-value: 2.29e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  930 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRSQL-EMEKRERRALERRISEMEEELKMLPDLK 1007
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLlETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 1578915130 1008 ADNQRLKDENGALIRVISKLSK 1029
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-331 8.32e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666     53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  119 LDIAEFLIGQGAHVGAVNSEGDTPldiaeeeameellqnevnrqgvdieaarkeeervmlrdarqwlnsghisdvrhaks 198
Cdd:COG0666    133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  199 ggtaLHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILG 278
Cdd:COG0666    157 ----LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  279 YLEELQKKQTLLHSEKRDKKSPLIESTANMENNQPQKAFKNKETLIIEPEKNA 331
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 1.81e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095    53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeervMLRDArqwlnsghISDVR 194
Cdd:PHA03095   128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 266
Cdd:PHA03095   182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                   ....*.
gi 1578915130  267 TAFDVA 272
Cdd:PHA03095   259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1578915130  127 GQGAHVGAVN 136
Cdd:pfam12796   82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-712 1.64e-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: 83.03  E-value: 1.64e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  658 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 712
Cdd:cd21944      3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.96e-06

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: 43.73  E-value: 5.96e-06
                            10        20
                    ....*....|....*....|....*....
gi 1578915130    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 1.39e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  139 GDTPLDIaeeeaMEELLQNEVNRQGVDIEAARKEEERVMLRDarqwlnsgHISDvrhaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192    169 GNTVLHI-----LVLQPNKTFACQMYDLILSYDKEDDLQPLD--------LVPN----NQGLTPFKLAAKEGNIVMFQHL 231


                   ..
gi 1578915130  219 IQ 220
Cdd:cd22192    232 VQ 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 866-1029 4.01e-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: 43.98  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  866 QERQSDTEDGSSKRETQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEDRKPY-SSRLEKDDSTDFKK---LYEQILAE 941
Cdd:COG4942     68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  942 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSQLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 1015
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                          170
                   ....*....|....
gi 1578915130 1016 ENGALIRVISKLSK 1029
Cdd:COG4942    228 LIARLEAEAAAAAE 241
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 73-242 4.07e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDN--------------EGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  139 GDTPLDIAEeeameellqnevnrqgvdIEAARKEEERVMLRDARQWLNSgHISDVRHAKS--------GGTALHVAAAKG 210
Cdd:TIGR00870  208 GNTLLHLLV------------------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKElevilnhqGLTPLKLAAKEG 268

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1578915130  211 YTEVLKLLIQAGYDVniKDYDGWT--PLHAAAHW 242
Cdd:TIGR00870  269 RIVLFRLKLAIKYKQ--KKFVAWPngQQLLSLYW 300
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 930-1029 2.29e-43

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: 152.46  E-value: 2.29e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  930 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRSQL-EMEKRERRALERRISEMEEELKMLPDLK 1007
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLlETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 1578915130 1008 ADNQRLKDENGALIRVISKLSK 1029
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-331 8.32e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 8.32e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666     53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  119 LDIAEFLIGQGAHVGAVNSEGDTPldiaeeeameellqnevnrqgvdieaarkeeervmlrdarqwlnsghisdvrhaks 198
Cdd:COG0666    133 LEIVKLLLEAGADVNAQDNDGNTP-------------------------------------------------------- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  199 ggtaLHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILG 278
Cdd:COG0666    157 ----LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  279 YLEELQKKQTLLHSEKRDKKSPLIESTANMENNQPQKAFKNKETLIIEPEKNA 331
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-269 3.05e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 3.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  119 LDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeervmlrdarqwlnsghisdvrhaks 198
Cdd:COG0666    199 LEIVKLLLEAGADVNAKDNDGKTALDL----------------------------------------------------- 225

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578915130  199 ggtalhvAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAF 269
Cdd:COG0666    226 -------AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 1.81e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095    53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeervMLRDArqwlnsghISDVR 194
Cdd:PHA03095   128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 266
Cdd:PHA03095   182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                   ....*.
gi 1578915130  267 TAFDVA 272
Cdd:PHA03095   259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1578915130  127 GQGAHVGAVN 136
Cdd:pfam12796   82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-712 1.64e-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: 83.03  E-value: 1.64e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  658 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 712
Cdd:cd21944      3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-229 5.32e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   77 LHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGahvgavnsegdtpldiaeeeameellq 156
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  157 nevnrqgvdieaarkeeervmlrdarqwlnsghisDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam12796   54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 50-236 3.58e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   50 SGDTDEVLKLLHR-GADINYANVDGLTALHQACIDDNVD--MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDI 121
Cdd:PHA03095    93 NATTLDVIKLLIKaGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VEL 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  122 AEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNRQGVDIEAARKEEERVMLRDA----------RQWLNSGHI 190
Cdd:PHA03095   170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCDPAATDMLGNTPLHSMAtgssckrslvLPLLIAGIS 249

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1578915130  191 SDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:PHA03095   250 INARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-240 9.68e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 9.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   55 EVLK-LLHRGADINYANVDGLTALH-----QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLI 126
Cdd:PHA03100    49 DVVKiLLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  127 GQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGVDIEAarkeEERVMLrdarqWLNSGHISDVRHAKsGGTALH 204
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GVDINA----KNRVNY-----LLSYGVPINIKDVY-GFTPLH 197

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1578915130  205 VAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 240
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-263 1.27e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   52 DTDEVLKLLHRGADINYANVDGL-TALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGA 130
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  131 HVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAArkeeervmlrdarqwlnsghiSDVRhaksGGTALHVAAAKg 210
Cdd:PHA02878   226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAK---------------------SYIL----GLTALHSSIKS- 279

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1578915130  211 yTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 263
Cdd:PHA02878   280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKRIKP 332
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-145 3.08e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 3.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA--CIDDNVDMVKFLVENGANINQ----------------PDNE 105
Cdd:PHA03100   112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVY 191

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1578915130  106 GWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-272 3.49e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.49e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMETVNKvGQTAFDVA 272
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 658-711 3.69e-15

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: 70.50  E-value: 3.69e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1578915130  658 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 711
Cdd:cd21945      1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 8.52e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 8.52e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-262 6.21e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 6.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  110 LHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdieaarkeeervmlrdarqwlnsgh 189
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL---------------------------------------------- 34

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  190 isdvrhaksggtalHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMETVN 262
Cdd:pfam12796   35 --------------HLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 8.38e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 8.38e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1578915130  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 252
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 661-713 8.44e-12

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


Pssm-ID: 412021  Cd Length: 53  Bit Score: 61.21  E-value: 8.44e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  661 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 713
Cdd:cd21946      1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-272 9.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 9.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02876   185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  127 GQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERVMLRDARQWLNSGHI-------SDVRHAKS- 198
Cdd:PHA02876   261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrtlimlgADVNAADRl 340

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  199 GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 272
Cdd:PHA02876   341 YITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-267 2.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   53 TDEVLKLLHRGADINYANV-DGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLI 126
Cdd:PHA03100    14 KVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  127 GQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieAARKEeervmlrdarqwLNSGHI--------SDVRHAKS 198
Cdd:PHA03100    94 EYGANVNAPDNNGITPLLY----------------------AISKK------------SNSYSIveylldngANVNIKNS 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  199 -GGTALHVAAAKGY--TEVLKLLIQAGYDVNIKD-------YD---------GWTPLHAAAHWGKEEACRILVDNLCDME 259
Cdd:PHA03100   140 dGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPN 219


                   ....*...
gi 1578915130  260 TVNKVGQT 267
Cdd:PHA03100   220 LVNKYGDT 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-310 4.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 4.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02874   103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  132 VGAVNSEGDTPLDIAeeeameellqnevnrqgvdIEAARKEEERVMLRdarqwlNSGHISDvrHAKSGGTALHVAAAKGY 211
Cdd:PHA02874   183 ANVKDNNGESPLHNA-------------------AEYGDYACIKLLID------HGNHIMN--KCKNGFTPLHNAIIHNR 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  212 TeVLKLLIQaGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVADEDI--LGYLEELQKKQT 288
Cdd:PHA02874   236 S-AIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYInkDPVIKDIIANAV 313

                          250       260
                   ....*....|....*....|..
gi 1578915130  289 LLHSEKRDKKSPLIESTANMEN 310
Cdd:PHA02874   314 LIKEADKLKDSDFLEHIEIKDN 335
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-287 1.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02874   131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  127 GQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVDIeaarkeeervmlrdarqWLNSGHISDvrHAKSGGTALH 204
Cdd:PHA02874   211 DHGNHIMNKCKNGFTPL------------HNAIihNRSAIEL-----------------LINNASIND--QDIDGSTPLH 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  205 VAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEAcrILVDNLCDMETVNKVGQtafdVADEDILGYLEEL 283
Cdd:PHA02874   260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIK 333


                   ....
gi 1578915130  284 QKKQ 287
Cdd:PHA02874   334 DNKE 337
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 659-708 3.99e-10

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: 56.04  E-value: 3.99e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1578915130  659 EVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKT 708
Cdd:cd22527      1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 661-707 6.06e-10

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: 55.43  E-value: 6.06e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1578915130  661 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 707
Cdd:cd21930      1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-298 1.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQAC-IDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDI 121
Cdd:PHA02876   311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  122 AEFLIGQGAhvgavnsegdtpldiaeeeameellqnevnrqgvDIEAArkeeervmlrdarqwlnsghisdvrhAKSGGT 201
Cdd:PHA02876   391 INTLLDYGA----------------------------------DIEAL--------------------------SQKIGT 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  202 ALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVAdediLG 278
Cdd:PHA02876   411 ALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LE 485

                          250       260
                   ....*....|....*....|..
gi 1578915130  279 YLEELqkkQTLLH--SEKRDKK 298
Cdd:PHA02876   486 YHGIV---NILLHygAELRDSR 504
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-145 3.07e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 3.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130   92 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 3.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 3.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130   59 LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAA 113
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-254 7.96e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 7.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   50 SGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQ 128
Cdd:PHA02874    11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  129 GAHVG----------AVNSEGDTPLDIAEEEAMEELLQNEVNRQGvDIEAARkeeervMLRDARQWLNsghISDVrhakS 198
Cdd:PHA02874    91 GVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLHYAIKKG-DLESIK------MLFEYGADVN---IEDD----N 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1578915130  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDN 254
Cdd:PHA02874   157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-268 9.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 9.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEF 124
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  125 LIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGVDIeaarkeeervmlrdARQWLNSGHISDVRHAKSgGTAL 203
Cdd:PHA02875    87 LLDLGKFADDVfYKDGMTPLHLATIL------------KKLDI--------------MKLLIARGADPDIPNTDK-FSPL 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 268
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 54-137 1.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   54 DEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG 133
Cdd:PHA03100   173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                   ....
gi 1578915130  134 AVNS 137
Cdd:PHA03100   253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-93 3.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1578915130   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLV 93
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-279 7.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 7.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   54 DEVLKLLHRGADINYANVDGLTALHQACI--------------------------------------------------- 82
Cdd:PHA02878    51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltnrykniqt 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   83 -----------DDNVD--MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaee 148
Cdd:PHA02878   131 idlvyidkkskDDIIEaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---- 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  149 eameellqnevnrqgvdiEAARKEEERVMlrdaRQWLNSGHISDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVN 226
Cdd:PHA02878   207 ------------------HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVN 262

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1578915130  227 IKDY-DGWTPLHAAAHwgKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878   263 AKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-141 9.13e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 9.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   45 LAAcsSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 124
Cdd:PTZ00322    89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*....
gi 1578915130  125 LIG--QGAHVGAVNSEGDT 141
Cdd:PTZ00322   167 LSRhsQCHFELGANAKPDS 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-291 2.11e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  157 NEVNRQGVDIEAARKEEERVMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666     12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578915130  237 HAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYLEEL--------QKKQTLLH 291
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLLLEAgadvnaqdNDGNTPLH 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 3.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1578915130  185 LNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 239
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-104 3.84e-07

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: 47.28  E-value: 3.84e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1578915130   72 DGLTALHQACID-DNVDMVKFLVENGANINQPDN 104
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-293 9.33e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 9.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  207 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKK 286
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   ....*..
gi 1578915130  287 QTLLHSE 293
Cdd:PTZ00322   170 HSQCHFE 176
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 52-143 1.04e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.99  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAAASCG------------ 117
Cdd:PHA02716   296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                           90       100
                   ....*....|....*....|....*...
gi 1578915130  118 --YLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02716   376 diRLDVIQCLISLGADITAVNCLGYTPL 403
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-279 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   67 NYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAH 131
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  132 VGAVNSEGDTPLDIAEeeameellqnevNRQGVDIEAARKEEERVMLRDA--RQWLNSGHISDVRHAKSGGTALHVAAAK 209
Cdd:PHA02878   111 NRNVEIFKIILTNRYK------------NIQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATEN 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  210 GYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878   179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-100 1.65e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 45.33  E-value: 1.65e-06
                           10        20
                   ....*....|....*....|....*....
gi 1578915130   72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-145 2.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.82  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   55 EVLKLL-HRGADINYANVDGLTALHQAC--IDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL------DIAEFL 125
Cdd:PHA02859   104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                           90       100
                   ....*....|....*....|
gi 1578915130  126 IGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA02859   179 TSLGIDINETNKSGYNCYDL 198
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-143 2.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   36 VKFDDGAVFLAACSSGDTDEVLK-LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAA 114
Cdd:PHA02875    97 VFYKDGMTPLHLATILKKLDIMKlLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                           90       100
                   ....*....|....*....|....*....
gi 1578915130  115 SCGYLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02875   177 AKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-280 4.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  232 GWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYL 280
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-308 5.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   56 VLKLLHRGADINY----ANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02876   124 ILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  132 VGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD------IEAARKE--EERVMLRDARQWLNSghISDVRHaksggTA 202
Cdd:PHA02876   204 VNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINkndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TP 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  203 LHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHaaahwgkeeacrILVDNLCDMETVNKVGQTAFDVADEDILgYLE 281
Cdd:PHA02876   277 LHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLY------------LMAKNGYDTENIRTLIMLGADVNAADRL-YIT 343

                          250       260
                   ....*....|....*....|....*..
gi 1578915130  282 ELQKKQTLlhSEKRDKKSPLIESTANM 308
Cdd:PHA02876   344 PLHQASTL--DRNKDIVITLLELGANV 368
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-292 5.90e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   86 VDMVKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrq 162
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPL------------------- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  163 gvdieaarkeeervmlrdarqwlnsghisdvrhaksggtalHVAAAKGYTE-VLKLLIQAGYDVNIKDYDGWTPLHA--A 239
Cdd:PHA03095    88 -----------------------------------------HLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylS 126

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578915130  240 AHWGKEEACRILVDNLCDMETVNKVGQTAFDV------ADEDILGYL-----EELQKK---QTLLHS 292
Cdd:PHA03095   127 GFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVELLRLLidagaDVYAVDdrfRSLLHH 193
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.96e-06

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: 43.73  E-value: 5.96e-06
                            10        20
                    ....*....|....*....|....*....
gi 1578915130    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 6.03e-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: 43.82  E-value: 6.03e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1578915130  199 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 1.39e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  139 GDTPLDIaeeeaMEELLQNEVNRQGVDIEAARKEEERVMLRDarqwlnsgHISDvrhaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192    169 GNTVLHI-----LVLQPNKTFACQMYDLILSYDKEDDLQPLD--------LVPN----NQGLTPFKLAAKEGNIVMFQHL 231


                   ..
gi 1578915130  219 IQ 220
Cdd:cd22192    232 VQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 185-301 2.35e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  185 LNSGHISDVRHAKsGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVD--NLCDMETVN 262
Cdd:PLN03192   545 LKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHAAG 623

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1578915130  263 KVGQTAfdvADEDILGYLEELQKKQTLLHSEKRDKKSPL 301
Cdd:PLN03192   624 DLLCTA---AKRNDLTAMKELLKQGLNVDSEDHQGATAL 659
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 41-99 2.44e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1578915130   41 GAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANI 99
Cdd:PLN03192   623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-227 2.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGA---DINYAnvDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  124 FLIGQGAHVGAVNSEGDTPLDIAEEEAmeellqnevnrqgvDIEAARkeeervMLrdarqwLNSGHISDVRHAKSGGTAL 203
Cdd:PHA02875   153 LLIDHKACLDIEDCCGCTPLIIAMAKG--------------DIAICK------ML------LDSGANIDYFGKNGCVAAL 206

                          170       180
                   ....*....|....*....|....
gi 1578915130  204 HVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:PHA02875   207 CYAIENNKIDIVRLFIKRGADCNI 230
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-237 4.51e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   53 TDEVLKLLHRGADINYANVDGLTALhqaC------IDDN--VDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE- 123
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  124 --FLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeervmlrdarqWLNSGHISDVrhaksggt 201
Cdd:PHA02798   128 llFMIENGADTTLLDKDGFTMLQV--------------------------------------YLQSNHHIDI-------- 161

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1578915130  202 alhvaaakgytEVLKLLIQAGYDVN-IKDYDGWTPLH 237
Cdd:PHA02798   162 -----------EIIKLLLEKGVDINtHNNKEKYDTLH 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-140 5.85e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 5.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   47 ACSSGDTDEVLKLLHRGADINYANVDGLTAL----------------HQACIDD---------------NVDMVKFLVEN 95
Cdd:PLN03192   565 AASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASISDphaagdllctaakrnDLTAMKELLKQ 644

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1578915130   96 GANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGD 140
Cdd:PLN03192   645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 6.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.02e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1578915130  218 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 272
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-132 8.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 8.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   42 AVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDD-NVDMVKFLVENGANINQPDNEGWIPLHAAasCGYLD 120
Cdd:PHA02876   411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                           90
                   ....*....|..
gi 1578915130  121 IAEFLIGQGAHV 132
Cdd:PHA02876   489 IVNILLHYGAEL 500
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-227 1.18e-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: 1.18e-04
                            10        20
                    ....*....|....*....|....*..
gi 1578915130   201 TALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 66-220 2.37e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.18  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   66 INYANVD----GLTALHQACIDDNVDMVKFLVENGANINQPDNE--------------GWIPLHAAASCGYLDIAEFLIG 127
Cdd:cd22196     83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  128 ---QGAHVGAVNSEGDTPL--------DIAEEEAMEELLQNEVNRQGVDIEAARKEEErvmlrdarqwlnsghISDvrha 196
Cdd:cd22196    163 nphSPADISARDSMGNTVLhalvevadNTPENTKFVTKMYNEILILGAKIRPLLKLEE---------------ITN---- 223

                          170       180
                   ....*....|....*....|....
gi 1578915130  197 KSGGTALHVAAAKGYTEVLKLLIQ 220
Cdd:cd22196    224 KKGLTPLKLAAKTGKIGIFAYILG 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 80-143 3.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 3.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578915130   80 ACIDD---NVDMVKFLVENGANIN-QPDNEGWIPLHAAASCGY---LDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02859    57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLL 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 866-1029 4.01e-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: 43.98  E-value: 4.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  866 QERQSDTEDGSSKRETQTDSVSRYDSSSTSSSDRYDSLLGRSASYSYLEDRKPY-SSRLEKDDSTDFKK---LYEQILAE 941
Cdd:COG4942     68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  942 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSQLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 1015
Cdd:COG4942    148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                          170
                   ....*....|....
gi 1578915130 1016 ENGALIRVISKLSK 1029
Cdd:COG4942    228 LIARLEAEAAAAAE 241
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-136 4.40e-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: 38.42  E-value: 4.40e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1578915130  105 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 136
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-145 5.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 5.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1578915130   89 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-129 5.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 5.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   55 EVLKLL-HRGADINYANVD-GLTALHQ-ACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAaascgYLD-------IA 122
Cdd:PHA02859    67 EILKFLiENGADVNFKTRDnNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-----YMCnfnvrinVI 141


                   ....*..
gi 1578915130  123 EFLIGQG 129
Cdd:PHA02859   142 KLLIDSG 148
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-145 6.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1578915130  109 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-227 1.14e-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: 37.24  E-value: 1.14e-03
                           10        20
                   ....*....|....*....|....*....
gi 1578915130  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-272 1.42e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   43 VFLAAcSSGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGAN-INQPDN----EGWIPLHAAASC 116
Cdd:cd22192     21 LLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  117 GYLDIAEFLIGQGAHVGAVNSEGdtpldiaeeeameellqnevnrqgvdieaarkeeeRVMLRDARQWLNSG-HIsdvrh 195
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATG-----------------------------------TFFRPGPKNLIYYGeHP----- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  196 aksggtaLHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHA-AAHWGKEEACRIL--------VDNLCDMETV-NKVG 265
Cdd:cd22192    140 -------LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTFACQMYdlilsydkEDDLQPLDLVpNNQG 212


                   ....*..
gi 1578915130  266 QTAFDVA 272
Cdd:cd22192    213 LTPFKLA 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-263 1.45e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1578915130  231 DGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 263
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 73-145 2.00e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNE-------------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV---N 136
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152


                   ....*....
gi 1578915130  137 SEGDTPLDI 145
Cdd:cd21882    153 SLGNTVLHA 161
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-268 2.73e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578915130  206 AAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 268
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 73-220 3.31e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIG---QGAHVGAV 135
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  136 NSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerVMLRDARqWLNSGHISDVRHAKsGGTALHVAAAKGYTEVL 215
Cdd:cd22193    156 DSRGNTVLHALVTVADNTKENTKFVTRMYDM---------ILIRGAK-LCPTVELEEIRNND-GLTPLQLAAKMGKIEIL 224


                   ....*
gi 1578915130  216 KLLIQ 220
Cdd:cd22193    225 KYILQ 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 181-251 3.93e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578915130  181 ARQWLNSGHISDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 251
Cdd:PTZ00322    98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 73-242 4.07e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   73 GLTALHQACIDDNVDMVKFLVENGANINQPDN--------------EGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  139 GDTPLDIAEeeameellqnevnrqgvdIEAARKEEERVMLRDARQWLNSgHISDVRHAKS--------GGTALHVAAAKG 210
Cdd:TIGR00870  208 GNTLLHLLV------------------MENEFKAEYEELSCQMYNFALS-LLDKLRDSKElevilnhqGLTPLKLAAKEG 268

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1578915130  211 YTEVLKLLIQAGYDVniKDYDGWT--PLHAAAHW 242
Cdd:TIGR00870  269 RIVLFRLKLAIKYKQ--KKFVAWPngQQLLSLYW 300
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
921-1015 8.43e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  921 SRLEKDDSTDFKKLY----------EQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSQLEMEKRERRALE 990
Cdd:COG4913    588 TRHEKDDRRRIRSRYvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE 667

                           90       100
                   ....*....|....*....|....*....
gi 1578915130  991 RRISEMEEELKML----PDLKADNQRLKD 1015
Cdd:COG4913    668 REIAELEAELERLdassDDLAALEEQLEE 696
PHA02946 PHA02946
ankyin-like protein; Provisional
 43-276 8.54e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 8.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130   43 VFLAACSSGDTDE--VLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCG--Y 118
Cdd:PHA02946    40 ILHAYCGIKGLDErfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  119 LDIAEFLIGQGAHV-GAVNSEGDTPLDIAEEEAMEELLQnevnRQGVDIEA------ARKEEERVMLRDARQ-----WLN 186
Cdd:PHA02946   120 IERINLLVQYGAKInNSVDEEGCGPLLACTDPSERVFKK----IMSIGFEArivdkfGKNHIHRHLMSDNPKastisWMM 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578915130  187 SGHISDVRHAKSGGTALHVAAAKGY--TEVLKLLIQAGyDVNIKDYDGWTPLhaaahwgkeeacRILVDNLCDMETVNKV 264
Cdd:PHA02946   196 KLGISPSKPDHDGNTPLHIVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL------------TLLIKTLSPAHLINKL 262

                          250
                   ....*....|..
gi 1578915130  265 GQTAFDVADEDI 276
Cdd:PHA02946   263 LSTSNVITDQTV 274
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH