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Conserved domains on  [gi|2462509476|ref|XP_054192714|]
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protein phosphatase 1 regulatory subunit 12B isoform X5 [Homo sapiens]

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 ...
 774-881 1.54e-38

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: 138.59  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 774 DYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEmknlhqLK 853
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 2462509476 854 QIQTLKQMNEQLQAENRALTRVVARLSE 881
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-159 5.28e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 5.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-- 122
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAae 228

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462509476 123 --DEGLVEHLELLQKKQNVLRSEKETRNKLIESDLNSKI 159
Cdd:COG0666   229 ngNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 501-557 5.08e-18

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: 78.79  E-value: 5.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509476 501 SSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRS 557
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 397-644 5.90e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  397 PTSPYISA--NRNSSPATSPITIGSSTSRGSQWQPASSCPAPISANTTASVHHGRTPhKSQADTTAEKTADNVSSSTPLC 474
Cdd:PHA03247  2745 PAGPATPGgpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP-WDPADPPAAVLAPAAALPPAAS 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  475 VITNRPLPSTANGV----TATPVLSITGTDSSVE--AREKRRSYLTPVRDEEAESLRKARSRQAR-QTRRSTQGVTLTDL 547
Cdd:PHA03247  2824 PAGPLPPPTSAQPTapppPPGPPPPSLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPD 2903

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  548 QEAERTFSRSRAERQAQEQPREKPTDTEGLEGSPEKHEPSAVPATEAGEGQ------QPW-GRSLDEEPICHRLRCPAQP 620
Cdd:PHA03247  2904 QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEpsgavpQPWlGALVPGRVAVPRFRVPQPA 2983

                          250       260
                   ....*....|....*....|....
gi 2462509476  621 DKPTTPASPSTSRPSLYTSSHLLW 644
Cdd:PHA03247  2984 PSREAPASSTPPLTGHSLSRVSSW 3007
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 774-881 1.54e-38

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: 138.59  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 774 DYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEmknlhqLK 853
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 2462509476 854 QIQTLKQMNEQLQAENRALTRVVARLSE 881
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-159 5.28e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 5.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-- 122
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAae 228

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462509476 123 --DEGLVEHLELLQKKQNVLRSEKETRNKLIESDLNSKI 159
Cdd:COG0666   229 ngNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 501-557 5.08e-18

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: 78.79  E-value: 5.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509476 501 SSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRS 557
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 4.79e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  53 LHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 2462509476 132 LL 133
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-133 5.06e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509476  57 AAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE-GLVEHLELL 133
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEnGFREVVQLL 167
PHA03247 PHA03247
large tegument protein UL36; Provisional
 397-644 5.90e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  397 PTSPYISA--NRNSSPATSPITIGSSTSRGSQWQPASSCPAPISANTTASVHHGRTPhKSQADTTAEKTADNVSSSTPLC 474
Cdd:PHA03247  2745 PAGPATPGgpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP-WDPADPPAAVLAPAAALPPAAS 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  475 VITNRPLPSTANGV----TATPVLSITGTDSSVE--AREKRRSYLTPVRDEEAESLRKARSRQAR-QTRRSTQGVTLTDL 547
Cdd:PHA03247  2824 PAGPLPPPTSAQPTapppPPGPPPPSLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPD 2903

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  548 QEAERTFSRSRAERQAQEQPREKPTDTEGLEGSPEKHEPSAVPATEAGEGQ------QPW-GRSLDEEPICHRLRCPAQP 620
Cdd:PHA03247  2904 QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEpsgavpQPWlGALVPGRVAVPRFRVPQPA 2983

                          250       260
                   ....*....|....*....|....
gi 2462509476  621 DKPTTPASPSTSRPSLYTSSHLLW 644
Cdd:PHA03247  2984 PSREAPASSTPPLTGHSLSRVSSW 3007
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 777-886 6.21e-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: 43.21  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 777 KLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEktsdrssVLEMEKRERRALERKMSEMEEEMKNLHqlKQIQ 856
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462509476 857 TLKQMNEQLQAENRALTRVVARLSESIESS 886
Cdd:COG4942   210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 9.12e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 9.12e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462509476   49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 1.51e-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: 42.31  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  53 LHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                          90
                  ....*....|....*..
gi 2462509476 122 A-DEGLVEHLELLQKKQ 137
Cdd:cd22192   219 AaKEGNIVMFQHLVQKR 235
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 793-871 1.87e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 1.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509476  793 LQEAQLELADIKSKLEKVAQQKQEktsdRSSVLEMEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA 871
Cdd:PRK11448   144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQ 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 779-885 8.34e-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: 40.04  E-value: 8.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  779 YESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKtsdrSSVLEMEKRERRALERKMSEMEEEM----KNLHQLKQ 854
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELEAELEELESRLEELEEQLetlrSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462509476  855 iQTLKQMNEQLQAENR--ALTRVVARLSESIES 885
Cdd:TIGR02168  394 -QIASLNNEIERLEARleRLEDRRERLQQEIEE 425
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 517-631 8.74e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 39.61  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 517 RDEEAESLRKAR--SRQARQTRRSTqgvTLTDLQEAERTFSRSRAER-QAQEQPREKPT---DTEGLEGSPEKHEPSAVP 590
Cdd:NF033838  366 RNEEKIKQAKAKveSKKAEATRLEK---IKTDRKKAEEEAKRKAAEEdKVKEKPAEQPQpapAPQPEKPAPKPEKPAEQP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462509476 591 ATEAGEGQQ---PWGRSLDEEPICHRLRCPAQPDKPTTPASPST 631
Cdd:NF033838  443 KAEKPADQQaeeDYARRSEEEYNRLTQQQPPKTEKPAQPSTPKT 486
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 774-881 1.54e-38

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: 138.59  E-value: 1.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 774 DYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEmknlhqLK 853
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 2462509476 854 QIQTLKQMNEQLQAENRALTRVVARLSE 881
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-159 5.28e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 5.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-- 122
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAae 228

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462509476 123 --DEGLVEHLELLQKKQNVLRSEKETRNKLIESDLNSKI 159
Cdd:COG0666   229 ngNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 501-557 5.08e-18

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: 78.79  E-value: 5.08e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462509476 501 SSVEAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRS 557
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 504-556 6.92e-18

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: 78.20  E-value: 6.92e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462509476 504 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSR 556
Cdd:cd21945     2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-133 9.49e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 9.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaE 195

                          90
                  ....*....|
gi 2462509476 124 EGLVEHLELL 133
Cdd:COG0666   196 NGHLEIVKLL 205
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 506-552 1.16e-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: 74.30  E-value: 1.16e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462509476 506 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAER 552
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 506-558 2.36e-16

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: 73.92  E-value: 2.36e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462509476 506 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 558
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-133 7.79e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 7.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  30 DARQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMD 109
Cdd:COG0666    68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                          90       100
                  ....*....|....*....|....*
gi 2462509476 110 IRNKLGQTPFDVA-DEGLVEHLELL 133
Cdd:COG0666   148 AQDNDGNTPLHLAaANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 4.79e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 4.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  53 LHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 2462509476 132 LL 133
Cdd:pfam12796  79 LL 80
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 504-553 7.09e-13

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


Pssm-ID: 412022  Cd Length: 50  Bit Score: 63.74  E-value: 7.09e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462509476 504 EAREKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERT 553
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-140 7.53e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 7.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 124
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          90
                  ....*....|....*.
gi 2462509476 125 GLVEHLELLQKKQNVL 140
Cdd:COG0666   262 AGAALIVKLLLLALLL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 5.09e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.09e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462509476  51 TALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSIL 101
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-112 5.12e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.12e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462509476  49 GATALHVAAAKGYSEVLRLLIQAGyELNVQDYdGWTPLHAAAHWGVKEACSILAEALCDMDIRN 112
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-89 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462509476  35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAA 89
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-133 1.08e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.49  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100
                  ....*....|....*....|
gi 2462509476 115 GQTPFDVA-DEGLVEHLELL 133
Cdd:COG0666   120 GETPLHLAaYNGNLEIVKLL 139
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 773-889 3.11e-06

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


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 48.75  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 773 RDYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEME------KRERRALERKMSEMEEEM 846
Cdd:pfam13851  43 ERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLEkelkdlKWEHEVLEQRFEKVERER 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462509476 847 KNLHQlKQIQTLKQMNEQLQAENRALTRVVARLSESIESSDTQ 889
Cdd:pfam13851 123 DELYD-KFEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQ 164
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-133 5.06e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509476  57 AAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE-GLVEHLELL 133
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEnGFREVVQLL 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-79 2.03e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 2.03e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462509476  42 DVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 79
Cdd:pfam12796  54 DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 2-122 6.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476   2 KDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQ 78
Cdd:PHA02878  118 KIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462509476  79 DYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-79 1.19e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.19e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462509476  49 GATALHVAAAK-GYSEVLRLLIQAGYELNVQD 79
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-122 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  40 IEDVrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPF 119
Cdd:PHA02874  152 IEDD----NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227


                  ...
gi 2462509476 120 DVA 122
Cdd:PHA02874  228 HNA 230
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 47-136 3.04e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  47 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQD-YDGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 117
Cdd:PHA02736   53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                          90       100
                  ....*....|....*....|
gi 2462509476 118 PFDVA-DEGLVEHLELLQKK 136
Cdd:PHA02736  129 PYYVAcERHDAKMMNILRAK 148
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-122 3.18e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 3.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462509476  47 RSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA03095  220 MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-122 3.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462509476  82 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA03247 PHA03247
large tegument protein UL36; Provisional
 397-644 5.90e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  397 PTSPYISA--NRNSSPATSPITIGSSTSRGSQWQPASSCPAPISANTTASVHHGRTPhKSQADTTAEKTADNVSSSTPLC 474
Cdd:PHA03247  2745 PAGPATPGgpARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP-WDPADPPAAVLAPAAALPPAAS 2823

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  475 VITNRPLPSTANGV----TATPVLSITGTDSSVE--AREKRRSYLTPVRDEEAESLRKARSRQAR-QTRRSTQGVTLTDL 547
Cdd:PHA03247  2824 PAGPLPPPTSAQPTapppPPGPPPPSLPLGGSVApgGDVRRRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPD 2903

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  548 QEAERTFSRSRAERQAQEQPREKPTDTEGLEGSPEKHEPSAVPATEAGEGQ------QPW-GRSLDEEPICHRLRCPAQP 620
Cdd:PHA03247  2904 QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEpsgavpQPWlGALVPGRVAVPRFRVPQPA 2983

                          250       260
                   ....*....|....*....|....
gi 2462509476  621 DKPTTPASPSTSRPSLYTSSHLLW 644
Cdd:PHA03247  2984 PSREAPASSTPPLTGHSLSRVSSW 3007
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-122 5.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 5.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509476  45 QARSGATALHVAAAKGYSeVLRLLIQaGYELNVQDYDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02874  219 KCKNGFTPLHNAIIHNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 777-886 6.21e-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: 43.21  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 777 KLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEktsdrssVLEMEKRERRALERKMSEMEEEMKNLHqlKQIQ 856
Cdd:COG4942   139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462509476 857 TLKQMNEQLQAENRALTRVVARLSESIESS 886
Cdd:COG4942   210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 9.12e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 9.12e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462509476   49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 769-879 9.41e-04

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


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.59  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 769 EDSNRDYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKV--------AQQKQEKTSDRSSVLE-MEKRERraLERKM 839
Cdd:pfam04012  96 EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLkarlkaakAQEAVQTSLGSLSTSSaTDSFER--IEEKI 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462509476 840 SEMEEEMKNLHQLKQIQTLKQMNEQLQAENRALTRVVARL 879
Cdd:pfam04012 174 EEREARADAAAELASAVDLDAKLEQAGIQMEVSEDVLARL 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-124 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  35 LNSGKIEDVRQARSgATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:PHA02874  111 LDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90
                  ....*....|
gi 2462509476 115 GQTPFDVADE 124
Cdd:PHA02874  190 GESPLHNAAE 199
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 1.51e-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: 42.31  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  53 LHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                          90
                  ....*....|....*..
gi 2462509476 122 A-DEGLVEHLELLQKKQ 137
Cdd:cd22192   219 AaKEGNIVMFQHLVQKR 235
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
780-889 1.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 780 ESALTENQKLKTKLQEAQLELADIKSKLEKV---AQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEMKNLHQlkQIQ 856
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQArseLEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE--ELE 118

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462509476 857 TLKQMNEQLQAENRALTRVVARLSESIESSDTQ 889
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 793-871 1.87e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 1.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462509476  793 LQEAQLELADIKSKLEKVAQQKQEktsdRSSVLEMEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA 871
Cdd:PRK11448   144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQ 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-117 1.89e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  18 QSRKEEEQQMLQDARQW---LNSGKIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLH 87
Cdd:PLN03192  484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462509476  88 AAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:PLN03192  564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 392-601 2.11e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.08  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  392 GRSSDPTSPYISA-------NRNSSPATSPITIGSSTSRGSQWQPASSCPAPISANTTASVHHGRTPHKSQADTTAEKTA 464
Cdd:PHA03307   233 GASSSDSSSSESSgcgwgpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSP 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  465 DNVSSSTP-----LCVITNRPLPSTANGVTATPVLSITGTDSSVEAREKRRSylTPVRDEEAESLRKARSRQARQTRRST 539
Cdd:PHA03307   313 RASSSSSSsressSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSS--PRKRPRPSRAPSSPAASAGRPTRRRA 390

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462509476  540 QGvtltdlQEAERTFSRSRAERQAQEQPREKPTDTEGLEGSPEKHEPsavPATEAGEgqqPW 601
Cdd:PHA03307   391 RA------AVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP---LLTPSGE---PW 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 773-890 2.13e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 773 RDYKKLYESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKTSDrssvLEMEKRERRALERKMSEMEEEMKnlHQL 852
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE----LEEAQAEEYELLAELARLEQDIA--RLE 308

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462509476 853 KQIQTLKQMNEQLQAENRALTRVVARLSESIESSDTQE 890
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-89 2.30e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476   1 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 64
Cdd:PLN03192  494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                          90       100
                  ....*....|....*....|....*
gi 2462509476  65 LRLLIQAGYELNVQDYDGWTPLHAA 89
Cdd:PLN03192  574 VLVLLKHACNVHIRDANGNTALWNA 598
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-157 2.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  47 RSGATALHVAAAKGYSE-VLRLLIQAGYELNVQDYDGWTPLHA-----AAHWGVKEacsILAEALCDMDIRNKLGQTPFD 120
Cdd:PHA03095   81 RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylsgfNINPKVIR---LLLRKGADVNALDLYGMTPLA 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462509476 121 V------ADeglVEHLELLQKKQNVLRSEKETRNKLIESDLNS 157
Cdd:PHA03095  158 VllksrnAN---VELLRLLIDAGADVYAVDDRFRSLLHHHLQS 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-117 2.81e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462509476  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-122 3.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462509476  68 LIQAGYE-LNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-113 4.01e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462509476  81 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 113
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PRK12704 PRK12704
phosphodiesterase; Provisional
 775-874 4.39e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 775 YKKLYESALTE-NQKLKTKLQEAQLELADIKSklEKVAQQKqEKTSDRSSVLEMEKRERRA----LERKMSEMEEEMKnl 849
Cdd:PRK12704   25 RKKIAEAKIKEaEEEAKRILEEAKKEAEAIKK--EALLEAK-EEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD-- 99

                          90       100
                  ....*....|....*....|....*
gi 2462509476 850 hqlKQIQTLKQMNEQLQAENRALTR 874
Cdd:PRK12704  100 ---RKLELLEKREEELEKKEKELEQ 121
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-77 4.67e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 4.67e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462509476  49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
777-890 7.36e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 777 KLYESALTEnqkLKTKLQEAQLELADIKSKLEKVAQQKQEKTSD-----RSSVLEMEKRERRALERKMSEMEEEMKNLHQ 851
Cdd:COG3206   215 KLLLQQLSE---LESQLAEARAELAEAEARLAALRAQLGSGPDAlpellQSPVIQQLRAQLAELEAELAELSARYTPNHP 291

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462509476 852 lkQIQTLKQMNEQLQAE-NRALTRVVARLSESIESSDTQE 890
Cdd:COG3206   292 --DVIALRAQIAALRAQlQQEAQRILASLEAELEALQARE 329
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 780-872 7.40e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 780 ESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQE-KTSDRSSVLEMEKRERRALERKMSEMEEEMKNLHQLKQIQTL 858
Cdd:PRK00409  523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602

                          90
                  ....*....|....
gi 2462509476 859 KQMNEQLQAENRAL 872
Cdd:PRK00409  603 SVKAHELIEARKRL 616
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 35-122 7.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDYDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:PHA02875   88 LDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167


                  ....*...
gi 2462509476 115 GQTPFDVA 122
Cdd:PHA02875  168 GCTPLIIA 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 779-885 8.34e-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: 40.04  E-value: 8.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476  779 YESALTENQKLKTKLQEAQLELADIKSKLEKVAQQKQEKtsdrSSVLEMEKRERRALERKMSEMEEEM----KNLHQLKQ 854
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELEAELEELESRLEELEEQLetlrSKVAQLEL 393

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462509476  855 iQTLKQMNEQLQAENR--ALTRVVARLSESIES 885
Cdd:TIGR02168  394 -QIASLNNEIERLEARleRLEDRRERLQQEIEE 425
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 789-888 8.61e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.49  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 789 LKTKLQEAQLELADIKSKLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEMKNLHQ-----LKQIQTLKQMNE 863
Cdd:pfam07888  32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREkheelEEKYKELSASSE 111

                          90       100
                  ....*....|....*....|....*....
gi 2462509476 864 QLQAENRALTRV----VARLSESIESSDT 888
Cdd:pfam07888 112 ELSEEKDALLAQraahEARIRELEEDIKT 140
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 517-631 8.74e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 39.61  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 517 RDEEAESLRKAR--SRQARQTRRSTqgvTLTDLQEAERTFSRSRAER-QAQEQPREKPT---DTEGLEGSPEKHEPSAVP 590
Cdd:NF033838  366 RNEEKIKQAKAKveSKKAEATRLEK---IKTDRKKAEEEAKRKAAEEdKVKEKPAEQPQpapAPQPEKPAPKPEKPAEQP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462509476 591 ATEAGEGQQ---PWGRSLDEEPICHRLRCPAQPDKPTTPASPST 631
Cdd:NF033838  443 KAEKPADQQaeeDYARRSEEEYNRLTQQQPPKTEKPAQPSTPKT 486
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 776-863 9.73e-03

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


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 37.28  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462509476 776 KKLYESALTENQKLKTKLQEAQLELADIKS---KLEKVAQQKQEKTSDRSSVLEMEKRERRALERKMSEMEEEMKNLHQL 852
Cdd:pfam10473  51 KAEVETLKAEIEEMAQNLRDLELDLVTLRSekeNLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEM 130

                          90
                  ....*....|.
gi 2462509476 853 KQIQtLKQMNE 863
Cdd:pfam10473 131 LQTQ-LKELNE 140
 
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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