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Conserved domains on  [gi|755519362|ref|XP_011248804|]
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protein phosphatase 1 regulatory subunit 12C isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 537-636 8.40e-39

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


:

Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 138.21  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  537 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 615
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 755519362  616 DNQRLKDENAALIRVISKLSK 636
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
IPD_PPP1R12 super family cl40436
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 377-430 2.15e-25

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.


The actual alignment was detected with superfamily member cd21945:

Pssm-ID: 424067  Cd Length: 54  Bit Score: 99.00  E-value: 2.15e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755519362 377 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 430
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-177 4.25e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   8 RYLLSHGANIAAVNSDGDLPLDLAesdAMEGllkaeitrrgvDVEAAKraeeelLLhdtrcwLNGGAMPEARHPRtGASA 87
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLA---AYNG-----------NLEIVK------LL------LEAGADVNAQDND-GNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  88 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA-----DEDVM 162
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengnLEIVK 236

                        170
                 ....*....|....*
gi 755519362 163 NLLEELAQKQEDLRN 177
Cdd:COG0666  237 LLLEAGADLNAKDKD 251
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 361-550 3.09e-03

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 361 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 440
Cdd:PRK12678  61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 441 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 520
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                        170       180       190
                 ....*....|....*....|....*....|
gi 755519362 521 DlvlESKQEHEEPDGGFRKMYTELRRENER 550
Cdd:PRK12678 212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 537-636 8.40e-39

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


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 138.21  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  537 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 615
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 755519362  616 DNQRLKDENAALIRVISKLSK 636
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 377-430 2.15e-25

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: 99.00  E-value: 2.15e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755519362 377 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 430
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-177 4.25e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   8 RYLLSHGANIAAVNSDGDLPLDLAesdAMEGllkaeitrrgvDVEAAKraeeelLLhdtrcwLNGGAMPEARHPRtGASA 87
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLA---AYNG-----------NLEIVK------LL------LEAGADVNAQDND-GNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  88 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA-----DEDVM 162
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengnLEIVK 236

                        170
                 ....*....|....*
gi 755519362 163 NLLEELAQKQEDLRN 177
Cdd:COG0666  237 LLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-139 8.04e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.04e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755519362   88 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 139
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-139 2.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755519362  67 RCWLNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 139
Cdd:PTZ00322  99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
543-636 3.82e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 543 ELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQRL 620
Cdd:COG2433  424 RLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLERL 498

                         90       100
                 ....*....|....*....|...
gi 755519362 621 KD-------ENAALIRVISKLSK 636
Cdd:COG2433  499 KElwklehsGELVPVKVVEKFTK 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 537-636 1.99e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   537 FRKMYTELRRENERLREALTETTLRLAQL-------KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKA 609
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLerriaatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEA 877

                           90       100       110
                   ....*....|....*....|....*....|.
gi 755519362   610 LSDLRADNQR----LKDENAALIRVISKLSK 636
Cdd:TIGR02168  878 LLNERASLEEalalLRSELEELSEELRELES 908
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 84-109 2.13e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|....*.
gi 755519362    84 GASALHVAAAKGYIEVMRLLLQAGYD 109
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 361-550 3.09e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 361 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 440
Cdd:PRK12678  61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 441 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 520
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                        170       180       190
                 ....*....|....*....|....*....|
gi 755519362 521 DlvlESKQEHEEPDGGFRKMYTELRRENER 550
Cdd:PRK12678 212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 549-626 8.37e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 8.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755519362  549 ERLREALTETTLRLAQLKVELERATQRQErfaERPALLELERFERRALERKAAELEEELKAlsdLRADNQRLKDENAA 626
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKA---QSQALAEAQQQELVALEGLAAELEEKQQE---LEAQLEQLQEKAAE 209
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 537-636 8.40e-39

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


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 138.21  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  537 FRKMYTELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 615
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 755519362  616 DNQRLKDENAALIRVISKLSK 636
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 377-430 2.15e-25

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: 99.00  E-value: 2.15e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755519362 377 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 430
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-177 4.25e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   8 RYLLSHGANIAAVNSDGDLPLDLAesdAMEGllkaeitrrgvDVEAAKraeeelLLhdtrcwLNGGAMPEARHPRtGASA 87
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLA---AYNG-----------NLEIVK------LL------LEAGADVNAQDND-GNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  88 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA-----DEDVM 162
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengnLEIVK 236

                        170
                 ....*....|....*
gi 755519362 163 NLLEELAQKQEDLRN 177
Cdd:COG0666  237 LLLEAGADLNAKDKD 251
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 380-426 1.78e-16

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: 73.53  E-value: 1.78e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755519362 380 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 426
Cdd:cd21930    1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 377-430 8.34e-16

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: 71.86  E-value: 8.34e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755519362 377 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKVAGK 430
Cdd:cd21944    3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-139 8.04e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.04e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755519362   88 LHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 139
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-165 5.36e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 5.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   9 YLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEITRRGVDVEAAKRAEEELLLHDTRC--------WLNGGAMPEARH 80
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALagdllvalLLLAAGADINAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  81 PRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA--- 157
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAaan 163


                 ....*....
gi 755519362 158 -DEDVMNLL 165
Cdd:COG0666  164 gNLEIVKLL 172
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 378-427 7.87e-12

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: 60.27  E-value: 7.87e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 755519362 378 DSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKV 427
Cdd:cd22527    1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 380-426 1.70e-11

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: 59.67  E-value: 1.70e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 755519362 380 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 426
Cdd:cd21946    1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAER 47
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-140 8.54e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 8.54e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755519362   84 GASALHVAAAKGYIEVMRLLLQAGyDTELRDgDGWTPLHAAAHWGVEDACRLLAEHG 140
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVKLLLEKG 84
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-136 2.04e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755519362   86 SALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLL 136
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-139 2.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755519362  67 RCWLNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEH 139
Cdd:PTZ00322  99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
82-124 3.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 3.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 755519362   82 RTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAA 124
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 92-194 3.56e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  92 AAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADE----DVMNLLEE 167
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEngfrEVVQLLSR 169

                         90       100
                 ....*....|....*....|....*..
gi 755519362 168 LAQKQEDLRNQKEGSQGRGQESQVPSS 194
Cdd:PTZ00322 170 HSQCHFELGANAKPDSFTGKPPSLEDS 196
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-114 4.17e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362    3 SAPCTRYLLSHGANIAAVNSDGDLPLDLAesdAMEGllkaeitrrgvDVEAAKraeeELLLHdtrcwlnggamPEARHPR 82
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLA---AKNG-----------HLEIVK----LLLEH-----------ADVNLKD 59

                          90       100       110
                  ....*....|....*....|....*....|..
gi 755519362   83 TGASALHVAAAKGYIEVMRLLLQAGYDTELRD 114
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 9-125 5.70e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   9 YLLSHGANIAAVNSDGDLPLDLA------ESDAMEGLLKaeitrRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPR 82
Cdd:PHA03100 126 YLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKLLID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755519362  83 tGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAA 125
Cdd:PHA03100 192 -GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-163 6.22e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   8 RYLLSHGANIAAVNSDGDLPLD--LAESDAMEGLLKAEItRRGVDVeAAKRAEEELLLH--------DTRC---WLNGGA 74
Cdd:PHA03095 136 RLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLI-DAGADV-YAVDDRFRSLLHhhlqsfkpRARIvreLIRAGC 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  75 MPEARHpRTGASALHVAAAKGYIE--VMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQR 152
Cdd:PHA03095 214 DPAATD-MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292

                        170
                 ....*....|.
gi 755519362 153 PCDLAdedVMN 163
Cdd:PHA03095 293 PLSLM---VRN 300
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 78-173 1.83e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  78 ARHPRTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDslthagqrpCDLA 157
Cdd:PLN03192 616 ISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD---------KANT 686

                         90
                 ....*....|....*..
gi 755519362 158 DEDVMNL-LEELAQKQE 173
Cdd:PLN03192 687 DDDFSPTeLRELLQKRE 703
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 86-154 2.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 2.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519362  86 SALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDsltHAGQRPC 154
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGC 202
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
543-636 3.82e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.69  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 543 ELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQRL 620
Cdd:COG2433  424 RLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLERL 498

                         90       100
                 ....*....|....*....|...
gi 755519362 621 KD-------ENAALIRVISKLSK 636
Cdd:COG2433  499 KElwklehsGELVPVKVVEKFTK 521
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 539-636 6.14e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 539 KMYTELRRENERLREALTETTLRLAQLKVELERATQRQERF-----AERPALLELERFERRALERKAAELEEELKALSDL 613
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                         90       100
                 ....*....|....*....|...
gi 755519362 614 RADNQRLKDENAALIRVISKLSK 636
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAE 241
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 84-114 9.16e-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: 36.88  E-value: 9.16e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755519362   84 GASALHVAAAK-GYIEVMRLLLQAGYDTELRD 114
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 515-634 1.08e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 515 RQHSQRDLVLESKQEHEEpdggfrKMYTELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFE-R 593
Cdd:COG1196  291 YELLAELARLEQDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaE 364

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755519362 594 RALERKAAELEEELKALSDLRADNQRLKDENAALIRVISKL 634
Cdd:COG1196  365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 82-144 1.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755519362  82 RTGASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMD 144
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 537-636 1.99e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362   537 FRKMYTELRRENERLREALTETTLRLAQL-------KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKA 609
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLerriaatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEA 877

                           90       100       110
                   ....*....|....*....|....*....|.
gi 755519362   610 LSDLRADNQR----LKDENAALIRVISKLSK 636
Cdd:TIGR02168  878 LLNERASLEEalalLRSELEELSEELRELES 908
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 512-635 2.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 512 QVRRQHSQRDLVLESKQEHEEpdggfrkmytELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERF 591
Cdd:COG1196  271 ELRLELEELELELEEAQAEEY----------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEE 337

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755519362 592 ERRALERKAAELEEELKALSDLRAD-NQRLKDENAALIRVISKLS 635
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELE 382
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 84-109 2.13e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|....*.
gi 755519362    84 GASALHVAAAKGYIEVMRLLLQAGYD 109
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 361-550 3.09e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 40.66  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 361 GSIVKPNVLTASAAPLADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQgvtltdlkEAEKVAGKVPEPEQPALP 440
Cdd:PRK12678  61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAA--------AAEAASAPEAAQARERRE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362 441 SLDPSRRPRVPGVENAEGPAQRAEAPEGQGQGPQAAREHRKAGHERRGPAEGEEAGPAERSPECSTvDGGSQVRRQHSQR 520
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGR-DGDDRDRRDRREQ 211

                        170       180       190
                 ....*....|....*....|....*....|
gi 755519362 521 DlvlESKQEHEEPDGGFRKMYTELRRENER 550
Cdd:PRK12678 212 G---DRREERGRRDGGDRRGRRRRRDRRDA 238
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 85-140 3.36e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 3.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755519362  85 ASALHVAAAKGYIEVMRLLLQAGYDTELRDGDGWTPLHAAAHWGVEDACRLLAEHG 140
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 550-627 5.50e-03

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


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 38.37  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519362  550 RLREALTETTLR---LAQLKVELERATQRQERF--AERPALLELERfERRALERKAAELEEELKALSDLradNQRLKDEN 624
Cdd:pfam08614  61 QLREELAELYRSrgeLAQRLVDLNEELQELEKKlrEDERRLAALEA-ERAQLEEKLKDREEELREKRKL---NQDLQDEL 136


                  ...
gi 755519362  625 AAL 627
Cdd:pfam08614 137 VAL 139
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-140 6.36e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.36e-03
                          10        20
                  ....*....|....*....|....*.
gi 755519362  116 DGWTPLHAAA-HWGVEDACRLLAEHG 140
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKG 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 116-144 8.34e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.34e-03
                           10        20
                   ....*....|....*....|....*....
gi 755519362   116 DGWTPLHAAAHWGVEDACRLLAEHGGGMD 144
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 549-626 8.37e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 8.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755519362  549 ERLREALTETTLRLAQLKVELERATQRQErfaERPALLELERFERRALERKAAELEEELKAlsdLRADNQRLKDENAA 626
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKA---QSQALAEAQQQELVALEGLAAELEEKQQE---LEAQLEQLQEKAAE 209
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-165 9.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 9.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755519362  117 GWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA----DEDVMNLL 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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