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Conserved domains on  [gi|1910901021|ref|XP_036137260|]
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protein lifeguard 1 [Molossus molossus]

Protein Classification

Pro-rich and LFG_like domain-containing protein( domain architecture ID 12172238)

Pro-rich and LFG_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LFG_like cd10428
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; ...
 147-363 1.17e-123

Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; Lifeguard (LFG) inhibits Fas-mediated apoptosis and interacts with the death receptor FasR/CD95/Apo1. LFG has been shown to interact with Bax and is supposed to be integral to cellular membranes such as the ER. A close homolog, PP1201 or RECS1, appears located in the Golgi compartment and also interacts with the Fas receptor CD95/Apo1. PP1201 is expressed in response to shear stress.


:

Pssm-ID: 198410  Cd Length: 217  Bit Score: 354.93  E-value: 1.17e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 147 NWDDKSIRQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCCGEFRRKHPWNLIA 226
Cdd:cd10428     1 PFDDKTIRRAFIRKVYSILTIQLLVTVAVIALFTFHDPVKKFVRKNPWLYYVSYIVFFITYIALACCEGLRRRFPWNLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 227 LSILTVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEI 306
Cdd:cd10428    81 LGIFTLAMSYMLGTIASFYDTKAVLIAVGITAVVCLGLTLFAFQTKYDFTSCGGVLFVLSIVLLIFGIVAIFFYVKWLHI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910901021 307 VYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd10428   161 VYASLGALLFSLYLAVDTQLLMGGRKYELSPEEYIFAALNIYVDIVNIFLYILQLIG 217
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 30-125 5.42e-12

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


:

Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 63.52  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  30 PPYPGAPYPQ-PPFQPSPYSQPGYPQGTPssyPQGGYPQDPYPQAGYPQGPYPQAGypqGPYPQGIYPQGPysQSPFPPN 108
Cdd:pfam15240  77 PPQGGKQKPQgPPPQGGPRPPPGKPQGPP---PQGGNQQQGPPPPGKPQGPPPQGG---GPPPQGGNQQGP--PPPPPGN 148

                          90
                  ....*....|....*....
gi 1910901021 109 PYGQPQ--AFPGQDPDSPQ 125
Cdd:pfam15240 149 PQGPPQrpPQPGNPQGPPQ 167
 
Name Accession Description Interval E-value
LFG_like cd10428
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; ...
 147-363 1.17e-123

Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; Lifeguard (LFG) inhibits Fas-mediated apoptosis and interacts with the death receptor FasR/CD95/Apo1. LFG has been shown to interact with Bax and is supposed to be integral to cellular membranes such as the ER. A close homolog, PP1201 or RECS1, appears located in the Golgi compartment and also interacts with the Fas receptor CD95/Apo1. PP1201 is expressed in response to shear stress.


Pssm-ID: 198410  Cd Length: 217  Bit Score: 354.93  E-value: 1.17e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 147 NWDDKSIRQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCCGEFRRKHPWNLIA 226
Cdd:cd10428     1 PFDDKTIRRAFIRKVYSILTIQLLVTVAVIALFTFHDPVKKFVRKNPWLYYVSYIVFFITYIALACCEGLRRRFPWNLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 227 LSILTVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEI 306
Cdd:cd10428    81 LGIFTLAMSYMLGTIASFYDTKAVLIAVGITAVVCLGLTLFAFQTKYDFTSCGGVLFVLSIVLLIFGIVAIFFYVKWLHI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910901021 307 VYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd10428   161 VYASLGALLFSLYLAVDTQLLMGGRKYELSPEEYIFAALNIYVDIVNIFLYILQLIG 217
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 155-362 1.67e-39

Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.


Pssm-ID: 460029  Cd Length: 207  Bit Score: 139.23  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 155 QAFIRKVFLVLTLQLSVTlSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIaLSCCGEFRRKHP--WNLIALSILTV 232
Cdd:pfam01027   1 RQFLRKVYGLLALGLLLT-AAVAYLVLSSPALLFPSLHPPLFWVLIIAPLGLLF-GALLLARKRKYSsnVALLLLLAFTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 233 SLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYASLG 312
Cdd:pfam01027  79 LMGLTLGPLLLVYTGAIIATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1910901021 313 ALLFTCFLAVDTQLLLgNKQLSLSPEEYVFAALNLYTDIINIFLYILTII 362
Cdd:pfam01027 159 VLLFSGFILYDTQRII-KRYGEYGDYDAILAALSLYLDFINLFLSLLRIL 207
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 154-364 1.88e-27

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 107.96  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 154 RQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCcGEFRRKHPWNLIALSILT-- 231
Cdd:COG0670    19 LRKVLRNTYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIAPLGLVFLLSK-LANRANSAAALALLFAYTal 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 232 --VSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYA 309
Cdd:COG0670    98 mgLTLSPILLVYTGLSGPASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNIFLQSPALSLAIS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910901021 310 SLGALLFTCFLAVDTQLLlgnKQLSLSPEEYVFAALNLYTDIINIFLYILTIIGR 364
Cdd:COG0670   178 VAGVLLFSGLTLYDTQRI---KHGYETNKQYIMAALSLYLDFINLFLSLLRLLGG 229
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 30-125 5.42e-12

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 63.52  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  30 PPYPGAPYPQ-PPFQPSPYSQPGYPQGTPssyPQGGYPQDPYPQAGYPQGPYPQAGypqGPYPQGIYPQGPysQSPFPPN 108
Cdd:pfam15240  77 PPQGGKQKPQgPPPQGGPRPPPGKPQGPP---PQGGNQQQGPPPPGKPQGPPPQGG---GPPPQGGNQQGP--PPPPPGN 148

                          90
                  ....*....|....*....
gi 1910901021 109 PYGQPQ--AFPGQDPDSPQ 125
Cdd:pfam15240 149 PQGPPQrpPQPGNPQGPPQ 167
PHA03377 PHA03377
EBNA-3C; Provisional
 25-135 4.26e-10

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 61.22  E-value: 4.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQPPfqPSPY---SQPGYPQGTPSSYPQGGYPQDPYPQagYPQGPYPQAGYPQgpYPQGIYPQGPYS 101
Cdd:PHA03377   754 PQAQQAPYPGYWEPRPP--QAPYlgyQEPQAQGVQVSSYPGYAGPWGLRAQ--HPRYRHSWAYWSQ--YPGHGHPQGPWA 827

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1910901021  102 QSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPP 135
Cdd:PHA03377   828 PRPPHLPPQWDGSAGHGQDQVSQFPHLQSETGPP 861
KLF1_2_4_N cd21972
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 24-130 1.30e-04

N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF1, KLF2, KLF4, and similar proteins.


Pssm-ID: 409230 [Multi-domain]  Cd Length: 194  Bit Score: 42.67  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  24 VPQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDP-----------YPQAGYPQGPYPQAGYPQ--GPY 90
Cdd:cd21972    32 VTSDNDNPPPPDPAYPPPESPESCSTVYDSDGCHPTPNAYCGPNGPglpghfllagnSPNLGPKIKTENQEQACMpvAGY 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1910901021  91 PQGIYPQGPYS--QSPFPPNPYGQPQAFPGQDPDSPQHGNYH 130
Cdd:cd21972   112 SGHYGPREPQRvpPAPPPPQYAGHFQYHGHFNMFSPPLRANH 153
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-153 1.46e-04

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.60  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYP--QP-PFQPSPYSQPGYPQGTPSSYPQggyPQDPYPQAG-YPQGPYPQAG-YPQGPYP----QGIY 95
Cdd:NF033839  383 PKPEVKPQPEKPKPevKPqPEKPKPEVKPQPEKPKPEVKPQ---PEKPKPEVKpQPEKPKPEVKpQPEKPKPevkpQPET 459

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910901021  96 PQGPYSQSPFPPNPYGQPQ-AFPGQDPDSPQH--------GNYHEEGPPSYYDNQDFPATNWDDKSI 153
Cdd:NF033839  460 PKPEVKPQPEKPKPEVKPQpEKPKPDNSKPQAddkkpstpNNLSKDKQPSNQASTNEKATNKPKKSL 526
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
25-74 2.52e-04

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 41.93  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYSQPgYPQGTPSSYPQGGYPQDPYPQAG 74
Cdd:COG3416    96 PPPAPQPSQPGPQQQPAPPSGPWGQA-APQQPGYGQPQYGQPAAGPSGGG 144
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 25-136 3.63e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIP-PYPGAPYPQPPFQPSPYSQ-PGYPQGTP-------SSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIY 95
Cdd:TIGR01628 383 RQLPMGsPMGGAMGQPPYYGQGPQQQfNGQPLGWPrmsmmptPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPV 462

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1910901021  96 PQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPS 136
Cdd:TIGR01628 463 MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQ 503
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-125 9.18e-04

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQ---PSPYSQPGYPQGTPSSYPQggyPQDPYPQA-GYPQGPYPQAG-YPQGPYPqGIYPQGP 99
Cdd:NF033839  295 PKPGMQPSPQPEKKEVKPEpetPKPEVKPQLEKPKPEVKPQ---PEKPKPEVkPQLETPKPEVKpQPEKPKP-EVKPQPE 370

                          90       100
                  ....*....|....*....|....*.
gi 1910901021 100 YSQSPFPPNPyGQPQAFPGQDPDSPQ 125
Cdd:NF033839  371 KPKPEVKPQP-ETPKPEVKPQPEKPK 395
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-125 2.24e-03

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.75  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPgaPYPQPPF----------QPSPYSQPGYPQgtPSSYPQGGYPQ---DPYPQAGYPQ-GPYPQAGYPQGPy 90
Cdd:NF033839  303 PQPEKKEVK--PEPETPKpevkpqlekpKPEVKPQPEKPK--PEVKPQLETPKpevKPQPEKPKPEvKPQPEKPKPEVK- 377

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1910901021  91 PQGIYPQGPYSQSPFPPNPYGQPQAFPGQDPDSPQ 125
Cdd:NF033839  378 PQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ 412
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-114 4.20e-03

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.98  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPF-QPSPYSQPGYPQGTPSsypqggyPQDPYPQAgypqGPYPQAGYPQGPyPQGIYPQGPYSQS 103
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKkEVKPEPETPKPEVKPQ-------LEKPKPEV----KPQPEKPKPEVK-PQLETPKPEVKPQ 357

                          90
                  ....*....|.
gi 1910901021 104 PFPPNPYGQPQ 114
Cdd:NF033839  358 PEKPKPEVKPQ 368
 
Name Accession Description Interval E-value
LFG_like cd10428
Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; ...
 147-363 1.17e-123

Proteins similar to and including lifeguard (LFG), a putative regulator of apoptosis; Lifeguard (LFG) inhibits Fas-mediated apoptosis and interacts with the death receptor FasR/CD95/Apo1. LFG has been shown to interact with Bax and is supposed to be integral to cellular membranes such as the ER. A close homolog, PP1201 or RECS1, appears located in the Golgi compartment and also interacts with the Fas receptor CD95/Apo1. PP1201 is expressed in response to shear stress.


Pssm-ID: 198410  Cd Length: 217  Bit Score: 354.93  E-value: 1.17e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 147 NWDDKSIRQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCCGEFRRKHPWNLIA 226
Cdd:cd10428     1 PFDDKTIRRAFIRKVYSILTIQLLVTVAVIALFTFHDPVKKFVRKNPWLYYVSYIVFFITYIALACCEGLRRRFPWNLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 227 LSILTVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEI 306
Cdd:cd10428    81 LGIFTLAMSYMLGTIASFYDTKAVLIAVGITAVVCLGLTLFAFQTKYDFTSCGGVLFVLSIVLLIFGIVAIFFYVKWLHI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1910901021 307 VYASLGALLFTCFLAVDTQLLLGNKQLSLSPEEYVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd10428   161 VYASLGALLFSLYLAVDTQLLMGGRKYELSPEEYIFAALNIYVDIVNIFLYILQLIG 217
GAAP_like cd10429
Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a ...
 150-363 2.06e-58

Golgi antiapoptotic protein; GAAP (or transmembrane BAX inhibitor motif containing 4) is a regulator of apoptosis that is related to the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Human GAAP has been linked to the modulation of intracellular fluxes of Ca(2+), by suppressing influx from the extracellular medium and reducing release from intracellular stores. A viral homolog (vaccinia virus vGAAP) acts similar to its human counterpart in inhibiting apoptosis.


Pssm-ID: 198411  Cd Length: 233  Bit Score: 189.35  E-value: 2.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 150 DKSIRQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCcgeFRRKHPWNLIALSI 229
Cdd:cd10429    23 EPEIRMAFLRKVYSILSVQLLATTAVSALFYLSPSIKTFVQSHPWLFLISLIGSLILLIALYW---KRHSHPVNLILLSL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 230 LTVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIF-IRNRILEIVY 308
Cdd:cd10429   100 FTLCEAYTVGLVVSFYDGKIVLQALILTLGVFVGLTAYTFQTKRDFSSFGALLFILLWALILLALIFQFfPYSPTFELVY 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910901021 309 ASLGALLFTCFLAVDTQLLLGNkqlsLSPEEYVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd10429   180 AGLGALLFSGYIVYDTQLIMKR----LSPDEYILAAISLYLDIINLFLSILRILA 230
BI-1-like cd06181
BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 ...
 153-363 1.55e-47

BAX inhibitor (BI)-1/YccA-like protein family; Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. This superfamily also contains the lifeguard(LFG)-like proteins and other subfamilies which appear to be related by common descent and also function as inhibitors of apoptosis. In plants, BI-1 like proteins play a role in pathogen resistance. A prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


Pssm-ID: 198409  Cd Length: 202  Bit Score: 159.89  E-value: 1.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 153 IRQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKgfvrqnvwtYYVSYAVFF-ISLIALSC-CGEFRRKHPWNLIALSIL 230
Cdd:cd06181     1 STKDFLRKVYMILALQLLLTAATATAFTVCDPGW---------YWSPALMGLlTSMLALMAtAAMIRAKMPVNLILLFGF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 231 TVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYAS 310
Cdd:cd06181    72 TGLMGYVVGPLLFFYGPTILLRALGGTALVFFGLTVYALQARKDFLFLGGPLMAGLGFLLLSFLLNTFFYSPWLHLVAAA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1910901021 311 LGALLFTCFLAVDTQLLLGNkqLSLSPEEYVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd06181   152 VGLVLFCGFLLYDTQLIIHK--AEVGPEDYINACISLYLDIINIFIRLLTILA 202
Bax1-I pfam01027
Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family ...
 155-362 1.67e-39

Inhibitor of apoptosis-promoting Bax1; Programmed cell-death involves a set of Bcl-2 family proteins, some of which inhibit apoptosis (Bcl-2 and Bcl-XL) and some of which promote it (Bax and Bak). Human Bax inhibitor, BI-1, is an evolutionarily conserved integral membrane protein containing multiple membrane-spanning segments predominantly localized to intracellular membranes. It has 6-7 membrane-spanning domains. The C termini of the mammalian BI-1 proteins are comprised of basic amino acids resembling some nuclear targeting sequences, but otherwise the predicted proteins lack motifs that suggest a function. As plant BI-1 appears to localize predominantly to the ER, we hypothesized that plant BI-1 could also regulate cell death triggered by ER stress. BI-1 appears to exert its effect through an interaction with calmodulin. The budding yeast member of this family has been found unexpectedly to encode a BH3 domain-containing protein (Ybh3p) that regulates the mitochondrial pathway of apoptosis in a phylogenetically conserved manner. Examination of the crystal structure of a bacterial member of this family shows that these proteins mediate a calcium leak across the membrane that is pH-dependent. Calcium homoeostasis balances passive calcium leak with active calcium uptake. The structure exists in a pore-closed and pore-open conformation, at pHs of 8 and 6 respectively, and the pore can be opened by intracrystalline transition; together these findings suggest that pH controls the conformational transition.


Pssm-ID: 460029  Cd Length: 207  Bit Score: 139.23  E-value: 1.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 155 QAFIRKVFLVLTLQLSVTlSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIaLSCCGEFRRKHP--WNLIALSILTV 232
Cdd:pfam01027   1 RQFLRKVYGLLALGLLLT-AAVAYLVLSSPALLFPSLHPPLFWVLIIAPLGLLF-GALLLARKRKYSsnVALLLLLAFTL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 233 SLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYASLG 312
Cdd:pfam01027  79 LMGLTLGPLLLVYTGAIIATAFLGTAAIFGGLSLYALTTKRDLSFLGGFLFAGLIGLIVASLVNIFLPSSALSLAISYLG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1910901021 313 ALLFTCFLAVDTQLLLgNKQLSLSPEEYVFAALNLYTDIINIFLYILTII 362
Cdd:pfam01027 159 VLLFSGFILYDTQRII-KRYGEYGDYDAILAALSLYLDFINLFLSLLRIL 207
YbhL COG0670
Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family ...
 154-364 1.88e-27

Integral membrane protein YbhL, putative Ca2+ regulator, Bax inhibitor (BI-1)/TMBIM family [Inorganic ion transport and metabolism];


Pssm-ID: 440434  Cd Length: 231  Bit Score: 107.96  E-value: 1.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 154 RQAFIRKVFLVLTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYYVSYAVFFISLIALSCcGEFRRKHPWNLIALSILT-- 231
Cdd:COG0670    19 LRKVLRNTYGLLALGLLLTALVAYLGMALPGLAALLFGSPGLFWVLLIAPLGLVFLLSK-LANRANSAAALALLFAYTal 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 232 --VSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYA 309
Cdd:COG0670    98 mgLTLSPILLVYTGLSGPASIAQAFGGTAATFGGLSLYGYTTKRDLSFLGSFLFMGLIGLIIASLVNIFLQSPALSLAIS 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1910901021 310 SLGALLFTCFLAVDTQLLlgnKQLSLSPEEYVFAALNLYTDIINIFLYILTIIGR 364
Cdd:COG0670   178 VAGVLLFSGLTLYDTQRI---KHGYETNKQYIMAALSLYLDFINLFLSLLRLLGG 229
BI-1-like_bacterial cd10432
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ...
 154-363 3.63e-23

Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


Pssm-ID: 198414  Cd Length: 211  Bit Score: 95.71  E-value: 3.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 154 RQAFIRKVFLVLTLQLSVTlSTVAVFTFVKEVKgFVRQNVWTYYVSYAVFFISLIALSccgeFRRKHP---WNLIALSIL 230
Cdd:cd10432     2 LRSFMKKVYGLMAAGLLLT-AVGAYVGASTPAL-LLIAGSPLMWVLLIAELALVFGLS----FRINKMsvaTALPLFFAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 231 TVSLSYMVGMIASFYNTEAVIMAVGITTTVCFTVVIFSMQTRYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYAS 310
Cdd:cd10432    76 AALTGLTLSPILLVYTGASIAQAFFTTAATFGGLSLYGYTTKKDLSFLGSFLFMGLIGLIIASLVNIFLQSSALQFAISA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1910901021 311 LGALLFTCFLAVDTQLL--LGNKQLSLSPEE-YVFAALNLYTDIINIFLYILTIIG 363
Cdd:cd10432   156 IGVLIFSGLIAYDTQRIkrMYEAGGGESGYKdAIMGALSLYLDFINLFLFLLRLFG 211
YccA_like cd10433
YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small ...
 197-363 4.56e-15

YccA-like proteins; A prokaryotic member of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.


Pssm-ID: 198415  Cd Length: 205  Bit Score: 73.00  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 197 YVSYAVFFISLIALSCCGEFRRKHPWNLIALSILT----VSLSYMVGMIASFYNTEAVIM-AVGITTTVCFTVVIFSMQT 271
Cdd:cd10433    35 IMGLLLTLVGAYGLLFLIEKTRNSAWGIVLVFAFTgfmgYTLGPILNMYLALPNGGQIIMtALGGTAAIFFGLSAYALTT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 272 RYDFTSCMGVLLVSMVVLIVFAVLCIFIRNRILEIVYASLGALLFTCFLAVDTQLLLGNKQLSlspeeYVFAALNLYTDI 351
Cdd:cd10433   115 KKDFSFLGGFLFVGAIVLLLAAVANIFLQIPALSLAISAAFVLFSSGFILYDTSRIIHGGETN-----YIMATVSLYVSI 189

                         170
                  ....*....|..
gi 1910901021 352 INIFLYILTIIG 363
Cdd:cd10433   190 YNLFVSLLNLLG 201
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 30-125 5.42e-12

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 63.52  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  30 PPYPGAPYPQ-PPFQPSPYSQPGYPQGTPssyPQGGYPQDPYPQAGYPQGPYPQAGypqGPYPQGIYPQGPysQSPFPPN 108
Cdd:pfam15240  77 PPQGGKQKPQgPPPQGGPRPPPGKPQGPP---PQGGNQQQGPPPPGKPQGPPPQGG---GPPPQGGNQQGP--PPPPPGN 148

                          90
                  ....*....|....*....
gi 1910901021 109 PYGQPQ--AFPGQDPDSPQ 125
Cdd:pfam15240 149 PQGPPQrpPQPGNPQGPPQ 167
PHA03377 PHA03377
EBNA-3C; Provisional
 25-135 4.26e-10

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 61.22  E-value: 4.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQPPfqPSPY---SQPGYPQGTPSSYPQGGYPQDPYPQagYPQGPYPQAGYPQgpYPQGIYPQGPYS 101
Cdd:PHA03377   754 PQAQQAPYPGYWEPRPP--QAPYlgyQEPQAQGVQVSSYPGYAGPWGLRAQ--HPRYRHSWAYWSQ--YPGHGHPQGPWA 827

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1910901021  102 QSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPP 135
Cdd:PHA03377   828 PRPPHLPPQWDGSAGHGQDQVSQFPHLQSETGPP 861
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 26-135 8.99e-10

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 56.97  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPGAPyPQPPFQPSPYS--QPGYPQGTP----SSYPQGGYPQ-DPYPQAGYPQGPYPQAGYPQGPYPQGIYPQG 98
Cdd:pfam15240  45 GPQGPPPGGFP-PQPPASDDPPGppPPGGPQQPPpqggKQKPQGPPPQgGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQG 123

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1910901021  99 PYSQSPFPPNPYGQPQAfpgqdPDSPQHGNyhEEGPP 135
Cdd:pfam15240 124 PPPQGGGPPPQGGNQQG-----PPPPPPGN--PQGPP 153
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 25-135 1.03e-09

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 56.97  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSsyPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQ--GIYPQGPYSQ 102
Cdd:pfam15240  62 DDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--PPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQggGPPPQGGNQQ 139

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1910901021 103 SPFPPNPyGQPQAFPGQdpdSPQHGNyhEEGPP 135
Cdd:pfam15240 140 GPPPPPP-GNPQGPPQR---PPQPGN--PQGPP 166
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 27-136 2.71e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 59.01  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  27 PSIPPYPGAPYPQPPFQPSPYSQP---------GYPQGTPSSY-PQGGYPQDPYPQAGYPQgPYPQAGY--PQGPYPQGI 94
Cdd:pfam03154 204 PSVPPQGSPATSQPPNQTQSTAAPhtliqqtptLHPQRLPSPHpPLQPMTQPPPPSQVSPQ-PLPQPSLhgQMPPMPHSL 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1910901021  95 YPQGPYSQSPFPPNPY------GQPQAFPGQDPDSPQHGNYHEEGPPS 136
Cdd:pfam03154 283 QTGPSHMQHPVPPQPFpltpqsSQSQVPPGPSPAAPGQSQQRIHTPPS 330
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-127 4.37e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 4.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPyPQPPFqpSPYSQPGYPQgTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSP 104
Cdd:PHA03247  2867 PSRSPAAKPAAP-ARPPV--RRLARPAVSR-STESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942

                           90       100
                   ....*....|....*....|...
gi 1910901021  105 FPPNPYGQPQAFPGQDPDSPQHG 127
Cdd:PHA03247  2943 LAPTTDPAGAGEPSGAVPQPWLG 2965
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 25-139 4.42e-08

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 51.67  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGtpSSYPqggypqdpypqagypqgPYPQAGYPQGPYPQGIYPQGPYSQSP 104
Cdd:pfam12868  49 RDYYEDPYSPSPYPPSPAGPYASQGQYYPET--NYFP-----------------PPPGSTPQPPVDPQPNAPPPPYNPAD 109

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1910901021 105 FPPNPYGQPQAFPGQDPDSPQHGNYHeeGPPSYYD 139
Cdd:pfam12868 110 YPPPPGAAPPPQPYQYPPPPGPDPYA--PRPRRAD 142
BI-1 cd10430
BAX inhibitor (BI)-1; Mammalian members of the BAX inhibitor (BI)-1 like family of small ...
 155-361 1.52e-07

BAX inhibitor (BI)-1; Mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. Their broad tissue distribution and high degree of conservation suggests an important regulatory role. In plants, BI-1 like proteins play a role in pathogen resistance.


Pssm-ID: 198412  Cd Length: 213  Bit Score: 51.45  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 155 QAFIRKVFLvlTLQLSVTLSTVAVFTFVKEVKGFVRQNVWTYyvsyaVFFISLIALSCCGEFRRKHPWNLIALSILT-VS 233
Cdd:cd10430     9 QQHLKKVYL--TLAVALLAAAVGAYVHMVINIGGLLTGLLSL-----GLSLWLAFTPSTGKNEPKRLGLLLGFAFLTgAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021 234 LSYMVGMIASFyNTEAVIMAVGITTTV--CFTVviFSMQTR---YDFtscMGVLLVSMV-VLIVFAVLCIFIRNRILEIV 307
Cdd:cd10430    82 LGPLLDLVIAI-NPSIIVTAFLGTAVIfaCFSL--AALLAKrreYLY---LGGLLSSALsILLLVSLANIFGGSKFLFQA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1910901021 308 YASLGALLFTCFLAVDTQLLLgnKQLSLSPEEYVFAALNLYTDIINIFLYILTI 361
Cdd:cd10430   156 ELYLGLLVFCGFVLFDTQMII--EKAENGDRDYIWHALDLFVDFVALFRRLLII 207
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-121 2.12e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPP----YPGAPYPQPPFQPSPYSQPGYPQGTPS---SYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQ 97
Cdd:PHA03247  2846 PPPSLPLggsvAPGGDVRRRPPSRSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                           90       100
                   ....*....|....*....|....
gi 1910901021   98 GPYSQSPFPPNPYGQPQAFPGQDP 121
Cdd:PHA03247  2926 PPQPQPPPPPPPRPQPPLAPTTDP 2949
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 33-121 2.73e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.78  E-value: 2.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   33 PGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQ---GPYPQAGYPQ---GPYPQGIYPQGPYSqspfP 106
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQqpvAPQPQYQQPQqpvAPQPQYQQPQQPVA----P 826

                           90
                   ....*....|....*
gi 1910901021  107 PNPYGQPQAFPGQDP 121
Cdd:PRK10263   827 QPQYQQPQQPVAPQP 841
dnaA PRK14086
chromosomal replication initiator protein DnaA;
25-149 2.78e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 52.14  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYSQPGYPQgtpssypqggYPQDPYPQAGYPQgpYPQAGYPqGPYPQGIYPQGPYSQS- 103
Cdd:PRK14086  106 SEPELPRPGRRPYEGYGGPRADDRPPGLPR----------QDQLPTARPAYPA--YQQRPEP-GAWPRAADDYGWQQQRl 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1910901021 104 -PFPPNPYGQP-QAFPGQDPDSPQHGNYHEEGPPSYYDnQDFPATNWD 149
Cdd:PRK14086  173 gFPPRAPYASPaSYAPEQERDREPYDAGRPEYDQRRRD-YDHPRPDWD 219
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 25-138 3.91e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQPPF------QPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGY----------PQGPYPQAGYPQG 88
Cdd:PRK10263   369 GEPVIAPAPEGYPQQSQYaqpavqYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPeqpaqqpyyaPAPEQPVAGNAWQ 448

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   89 PYPQGIY--------PQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHG--NYHEEGPPSYY 138
Cdd:PRK10263   449 AEEQQSTfapqstyqTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVveETKPARPPLYY 508
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2-104 4.08e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 52.01  E-value: 4.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021    2 PHEKSFLVSGDNYPPPNPGYPGVPQPSIPPYPGAPY-----PQPPFQPSP-YSQPGYPQGTPSSYPQGGYPQDPYPQAGY 75
Cdd:PRK10263   740 PHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVAPQpqyqqPQQPVAPQPqYQQPQQPVAPQPQYQQPQQPVAPQPQYQQ 819

                           90       100
                   ....*....|....*....|....*....
gi 1910901021   76 PQGPYPqagyPQGPYPQgiyPQGPYSQSP 104
Cdd:PRK10263   820 PQQPVA----PQPQYQQ---PQQPVAPQP 841
dnaA PRK14086
chromosomal replication initiator protein DnaA;
26-136 4.75e-07

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 51.75  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPGAP-----YPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQ-DPYPQagyPQGPYPQAGYPQGPYPQGIYPQGP 99
Cdd:PRK14086  130 PPGLPRQDQLPtarpaYPAYQQRPEPGAWPRAADDYGWQQQRLGFPPrAPYAS---PASYAPEQERDREPYDAGRPEYDQ 206

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1910901021 100 YSQSPFPPNP-YGQPQAFPGQDPD-SPQHGNYHEEGPPS 136
Cdd:PRK14086  207 RRRDYDHPRPdWDRPRRDRTDRPEpPPGAGHVHRGGPGP 245
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 32-147 2.53e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 49.69  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   32 YPGAPYPQPPFQPSPYSQPGYpqgTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPNPYG 111
Cdd:PTZ00395   399 QSNAAQSNAGFSNAGYSNPGN---SNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLSNAPPS 475

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1910901021  112 QPQAFPGQDPDSPQHGNYHEEGPPSYYDNQdfPATN 147
Cdd:PTZ00395   476 SAKDHHSAYHAAYQHRAANQPAANLPTANQ--PAAN 509
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 24-121 2.73e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  24 VPQPSiPPYPGAPYPQPPFQPSPYSQPG---YPQGTPSSYP-QGGYP--QDPYPQAGYPQGpyPQAGYPQGPYPQGIYPQ 97
Cdd:pfam03154 242 LPSPH-PPLQPMTQPPPPSQVSPQPLPQpslHGQMPPMPHSlQTGPShmQHPVPPQPFPLT--PQSSQSQVPPGPSPAAP 318

                          90       100
                  ....*....|....*....|....
gi 1910901021  98 GPYSQSPFPPNPygQPQAFPGQDP 121
Cdd:pfam03154 319 GQSQQRIHTPPS--QSQLQSQQPP 340
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 31-130 3.18e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 49.30  E-value: 3.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   31 PYPGAPYPQPPFQPSPYSQPGYP--QGTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPN 108
Cdd:PTZ00395   383 PHSNASYNCAAYSNAAQSNAAQSnaGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNLPYSNT 462

                           90       100
                   ....*....|....*....|....
gi 1910901021  109 PYGQPqAFPGQDPDSP--QHGNYH 130
Cdd:PTZ00395   463 PYSNA-PLSNAPPSSAkdHHSAYH 485
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 24-135 3.89e-06

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 48.88  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  24 VPQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGY--------PQDPYPQAGYPQGPYPQAGYPQGPYPQGIY 95
Cdd:pfam09770 219 AQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGhpvtilqrPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQ 298

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1910901021  96 P----QGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPP 135
Cdd:pfam09770 299 PtqilQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQ 342
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 24-137 5.96e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.54  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   24 VPQPSIP--PYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYP---------------QAGYPQGPYPQAGYP 86
Cdd:PRK10263   353 PAQPTVAwqPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQpqqpyyapaaeqpaqQPYYAPAPEQPAQQP 432

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1910901021   87 QgPYPQGIYP------QGPYSQSPFPPNPYGQP-QAFPGQDPDSPQHGNYHEEGPPSY 137
Cdd:PRK10263   433 Y-YAPAPEQPvagnawQAEEQQSTFAPQSTYQTeQTYQQPAAQEPLYQQPQPVEQQPV 489
PHA03377 PHA03377
EBNA-3C; Provisional
 38-152 5.99e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 48.13  E-value: 5.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   38 PQPPFQPSPYS-QPGY--PQGT------PSSYPQGGyPQDPYPqaGYPQGPYPQAGYP--QGPYPqgiyPQGPYSQSPFP 106
Cdd:PHA03377   708 SMSPTQPISHEeQPRYedPDDPldlslhPDQAPPPS-HQAPYS--GHEEPQAQQAPYPgyWEPRP----PQAPYLGYQEP 780

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1910901021  107 PNPYGQPQAFPGQD---PDSPQHGNY-HEEGPPSYYDNQDFPATNWDDKS 152
Cdd:PHA03377   781 QAQGVQVSSYPGYAgpwGLRAQHPRYrHSWAYWSQYPGHGHPQGPWAPRP 830
PHA03378 PHA03378
EBNA-3B; Provisional
 25-117 7.97e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYP-----GAPYPQPPFQPSPySQPGYPQGTPS-SYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGiYPQG 98
Cdd:PHA03378  705 RPPAAPPGRaqrpaAATGRARPPAAAP-GRARPPAAAPGrARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQP-PPQA 782

                          90       100
                  ....*....|....*....|..
gi 1910901021  99 PYSQSPFP---PNPYGQPQAFP 117
Cdd:PHA03378  783 PPAPQQRPrgaPTPQPPPQAGP 804
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 30-89 8.01e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.15  E-value: 8.01e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   30 PPYPGAPYPQPPFQPSPYSQPGYpQGTPSSYPQggYPQDPYPQAGYPQGPYPQAGYPQGP 89
Cdd:PTZ00395   417 PGNSNPGYNNAPNSNTPYNNPPN-SNTPYSNPP--NSNPPYSNLPYSNTPYSNAPLSNAP 473
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 46-156 1.13e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 47.38  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   46 PYSQPGYpqgTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPNPYGQPqafpgqdPDSpq 125
Cdd:PTZ00395   383 PHSNASY---NCAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNP-------PNS-- 450

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1910901021  126 hgnyheeGPPsyYDNQDFPATNWDDKSIRQA 156
Cdd:PTZ00395   451 -------NPP--YSNLPYSNTPYSNAPLSNA 472
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 24-141 1.27e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.39  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   24 VPQPSIP-PYPGAPYPQPPFQPSPYSQPGYP--QGTPSSYPQggYPQDPYPQAGYpQGPYPQAGYPQGPYPQGIYPQGPY 100
Cdd:PRK10263   341 TQTPPVAsVDVPPAQPTVAWQPVPGPQTGEPviAPAPEGYPQ--QSQYAQPAVQY-NEPLQQPVQPQQPYYAPAAEQPAQ 417

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1910901021  101 SQSPFPPNPYGQPQAFPGQDPDSPQHGN-YHEEGPPSYYDNQ 141
Cdd:PRK10263   418 QPYYAPAPEQPAQQPYYAPAPEQPVAGNaWQAEEQQSTFAPQ 459
PHA03378 PHA03378
EBNA-3B; Provisional
 25-127 1.60e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPyPGAPYPQPPFQPSPYSQPGyPQGTPSSY-PQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQS 103
Cdd:PHA03378  701 PTPMRPP-AAPPGRAQRPAAATGRARP-PAAAPGRArPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQP 778

                          90       100
                  ....*....|....*....|....*.
gi 1910901021 104 P--FPPNPYGQPQAFPGQDPdSPQHG 127
Cdd:PHA03378  779 PpqAPPAPQQRPRGAPTPQP-PPQAG 803
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 31-159 1.79e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 1.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   31 PYPGAPYPQPPFQPSPYSQ-----PGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAgyPQGPYPQGIYPQGPYSQSPF 105
Cdd:PRK10263   716 PAGANPFSLDDFEFSPMKAllddgPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQQPVA--PQPQYQQPQQPVAPQPQYQQ 793

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1910901021  106 PPNPYG-QPQAFPGQDPDSPQHGNYHEEGP----PSYYDNQDFPATNWDDKSIRQAFIR 159
Cdd:PRK10263   794 PQQPVApQPQYQQPQQPVAPQPQYQQPQQPvapqPQYQQPQQPVAPQPQDTLLHPLLMR 852
PHA03369 PHA03369
capsid maturational protease; Provisional
 30-113 1.84e-05

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 46.53  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  30 PPYPGAPypQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPNP 109
Cdd:PHA03369  366 VAVIAAP--QTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNP 443


                  ....
gi 1910901021 110 YGQP 113
Cdd:PHA03369  444 YVMP 447
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 21-125 2.30e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  21 YPGVP-------QPSIPPyPGAPYPQPPFQPSPYSQPGY---PQGTPSSYPQGGYPQDPYP-QAGYPQGPYPQAgypqgP 89
Cdd:pfam03154 222 QSTAAphtliqqTPTLHP-QRLPSPHPPLQPMTQPPPPSqvsPQPLPQPSLHGQMPPMPHSlQTGPSHMQHPVP-----P 295

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1910901021  90 YPQGIYPQGPYSQSPFPPNPY--GQPQAFPGQDPDSPQ 125
Cdd:pfam03154 296 QPFPLTPQSSQSQVPPGPSPAapGQSQQRIHTPPSQSQ 333
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 26-116 2.71e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.22  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   26 QPSIPPYPGAPYPQPPFQPSPYSQpgypqgTPSSYPqggypqdPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPf 105
Cdd:PTZ00395   408 GFSNAGYSNPGNSNPGYNNAPNSN------TPYNNP-------PNSNTPYSNPPNSNPPYSNLPYSNTPYSNAPLSNAP- 473

                           90
                   ....*....|.
gi 1910901021  106 PPNPYGQPQAF 116
Cdd:PTZ00395   474 PSSAKDHHSAY 484
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-136 3.35e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQP-----------PFQPSPYSQPGYPQ-GTPSSYPQGGYPQDPYPQAGYPQgPYPQAGYPQGPYPQ 92
Cdd:PHA03247  2834 AQPTAPPPPPGPPPPSlplggsvapggDVRRRPPSRSPAAKpAAPARPPVRRLARPAVSRSTESF-ALPPDQPERPPQPQ 2912

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1910901021   93 GIYPQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPS 136
Cdd:PHA03247  2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 30-133 8.09e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 44.68  E-value: 8.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   30 PPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPqggYPQDPYPQAGYPQGP------YP---QAGY-------PQGPYPQG 93
Cdd:PTZ00395   427 APNSNTPYNNPPNSNTPYSNPPNSNPPYSNLP---YSNTPYSNAPLSNAPpssakdHHsayHAAYqhraanqPAANLPTA 503

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1910901021   94 IYPQG-------------PYSQSPFPPNPYGQpQAFPGQDPDSPQHGNYHEEG 133
Cdd:PTZ00395   504 NQPAAnnfhgaagnsvgnPFASRPFGSAPYGG-NAATTADPNGIAKREDHPEG 555
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 67-154 1.13e-04

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.33  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  67 QDPYPQAGYPQGPYPQAG-YPQGPYPQGIYPQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPSYYDNQDFPA 145
Cdd:pfam15240  26 EDSPSLISEEEGQSQQGGqGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPP 105


                  ....*....
gi 1910901021 146 TNWDDKSIR 154
Cdd:pfam15240 106 PQGGNQQQG 114
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 26-145 1.15e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPGAPYPQPPFQPSPYSQ---PGYPQGTPSSYPQGGYPQDPYPQAGYPQGPyPQAGYPQGP--YPQGI-YPQGP 99
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQaatAGPTPSAPSVPPQGSPATSQPPNQTQSTAA-PHTLIQQTPtlHPQRLpSPHPP 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1910901021 100 YSQSPFPPNPygqPQAFPGQDPDSPQHGnyheEGPPSYYDNQDFPA 145
Cdd:pfam03154 249 LQPMTQPPPP---SQVSPQPLPQPSLHG----QMPPMPHSLQTGPS 287
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 23-156 1.28e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  23 GVPQPSIPPYPGAPYPQPP--FQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGypQGPYPQAGYPQGPYPQgiYPQGPY 100
Cdd:PRK07764  674 GGAAPAAPPPAPAPAAPAApaGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG--ASAPSPAADDPVPLPP--EPDDPP 749

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1910901021 101 SQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPSYydnqDFPATNWDDKSIRQA 156
Cdd:PRK07764  750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA----EDDAPSMDDEDRRDA 801
KLF1_2_4_N cd21972
N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel ...
 24-130 1.30e-04

N-terminal domain of Kruppel-like factor (KLF) 1, KLF2, KLF4, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF1, KLF2, KLF4, and similar proteins.


Pssm-ID: 409230 [Multi-domain]  Cd Length: 194  Bit Score: 42.67  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  24 VPQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDP-----------YPQAGYPQGPYPQAGYPQ--GPY 90
Cdd:cd21972    32 VTSDNDNPPPPDPAYPPPESPESCSTVYDSDGCHPTPNAYCGPNGPglpghfllagnSPNLGPKIKTENQEQACMpvAGY 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1910901021  91 PQGIYPQGPYS--QSPFPPNPYGQPQAFPGQDPDSPQHGNYH 130
Cdd:cd21972   112 SGHYGPREPQRvpPAPPPPQYAGHFQYHGHFNMFSPPLRANH 153
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-124 1.39e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQPPFQPSPYSQPGYPqgtpssyPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSP 104
Cdd:PHA03247  2564 PDRSVPPPRPAPRPSEPAVTSRARRPDAP-------PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAAN 2636

                           90       100
                   ....*....|....*....|
gi 1910901021  105 FPPNPYGQPQAFPGQDPDSP 124
Cdd:PHA03247  2637 EPDPHPPPTVPPPERPRDDP 2656
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-153 1.46e-04

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 43.60  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYP--QP-PFQPSPYSQPGYPQGTPSSYPQggyPQDPYPQAG-YPQGPYPQAG-YPQGPYP----QGIY 95
Cdd:NF033839  383 PKPEVKPQPEKPKPevKPqPEKPKPEVKPQPEKPKPEVKPQ---PEKPKPEVKpQPEKPKPEVKpQPEKPKPevkpQPET 459

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1910901021  96 PQGPYSQSPFPPNPYGQPQ-AFPGQDPDSPQH--------GNYHEEGPPSYYDNQDFPATNWDDKSI 153
Cdd:NF033839  460 PKPEVKPQPEKPKPEVKPQpEKPKPDNSKPQAddkkpstpNNLSKDKQPSNQASTNEKATNKPKKSL 526
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 25-150 1.58e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAP----YPQPPFQPSPYS-----QPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYP--QAGYPQGPYPQG 93
Cdd:PRK07764  613 ARPAAPAAPAAPaapaPAGAAAAPAEASaapapGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPaaPPPAPAPAAPAA 692

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1910901021  94 IYPQGPYSQSPFPPN---------PYGQPQAfPGQDPDSPQHGNYHEEGPPSYYDNQDFPATNWDD 150
Cdd:PRK07764  693 PAGAAPAQPAPAPAAtppagqaddPAAQPPQ-AAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757
PHA03247 PHA03247
large tegument protein UL36; Provisional
 24-125 1.88e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   24 VPQPSIPPYPGAPYPQPPFQPSPysQPGYPQGTPSSYPQGgYPQDPYPQAGY--PQGPYPQAGYPQGPYPQGIYPQGPYS 101
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLP--PPTSAQPTAPPPPPG-PPPPSLPLGGSvaPGGDVRRRPPSRSPAAKPAAPARPPV 2883

                           90       100
                   ....*....|....*....|....
gi 1910901021  102 QSPFPPNPYGQPQAFPgQDPDSPQ 125
Cdd:PHA03247  2884 RRLARPAVSRSTESFA-LPPDQPE 2906
COG3416 COG3416
Uncharacterized conserved protein, DUF2076 domain [Function unknown];
25-74 2.52e-04

Uncharacterized conserved protein, DUF2076 domain [Function unknown];


Pssm-ID: 442642 [Multi-domain]  Cd Length: 237  Bit Score: 41.93  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYSQPgYPQGTPSSYPQGGYPQDPYPQAG 74
Cdd:COG3416    96 PPPAPQPSQPGPQQQPAPPSGPWGQA-APQQPGYGQPQYGQPAAGPSGGG 144
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 25-136 3.63e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIP-PYPGAPYPQPPFQPSPYSQ-PGYPQGTP-------SSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIY 95
Cdd:TIGR01628 383 RQLPMGsPMGGAMGQPPYYGQGPQQQfNGQPLGWPrmsmmptPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPV 462

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1910901021  96 PQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPS 136
Cdd:TIGR01628 463 MYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQ 503
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 24-127 5.64e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 5.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  24 VPQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAgyPQGPYPQGIYPQGPYSQS 103
Cdd:PRK07764  405 APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA--QPAPAPAAAPEPTAAPAP 482

                          90       100
                  ....*....|....*....|....
gi 1910901021 104 PFPPNPYGQPQAFPGQDPDSPQHG 127
Cdd:PRK07764  483 APPAAPAPAAAPAAPAAPAAPAGA 506
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 26-113 9.02e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 40.67  E-value: 9.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPG-------APYPQPPFQPSPYS----QPGYPQgtpssyPQGGYPQDPYPQAGYPQGPYPQagypQGPYPQGI 94
Cdd:pfam15991 184 NKSTAQYPPsgqlfypTHQYLPPPQTQGQAdarlQTIYPQ------PGYALPLQQQYEHANQPSPFVS----SSPLKQMQ 253

                          90
                  ....*....|....*....
gi 1910901021  95 YPQGPYSQSPFPPNPYGQP 113
Cdd:pfam15991 254 SPKAGPGPQPMQLSVLHIP 272
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-125 9.18e-04

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQ---PSPYSQPGYPQGTPSSYPQggyPQDPYPQA-GYPQGPYPQAG-YPQGPYPqGIYPQGP 99
Cdd:NF033839  295 PKPGMQPSPQPEKKEVKPEpetPKPEVKPQLEKPKPEVKPQ---PEKPKPEVkPQLETPKPEVKpQPEKPKP-EVKPQPE 370

                          90       100
                  ....*....|....*....|....*.
gi 1910901021 100 YSQSPFPPNPyGQPQAFPGQDPDSPQ 125
Cdd:NF033839  371 KPKPEVKPQP-ETPKPEVKPQPEKPK 395
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 43-119 1.10e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 40.96  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910901021  43 QPSPYSQPGYPQGTPS-SYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQspfPPNPYGQPQAFPGQ 119
Cdd:PRK13729  120 VKALGANPVTATGEPVpQMPASPPGPEGEPQPGNTPVSFPPQGSVAVPPPTAFYPGNGVTP---PPQVTYQSVPVPNR 194
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 27-113 1.12e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.91  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  27 PSIPPYPGAPYPQP-PFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPf 105
Cdd:pfam03154 408 PSAHPPPLQLMPQSqQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTS- 486


                  ....*...
gi 1910901021 106 PPNPYGQP 113
Cdd:pfam03154 487 SAMPGIQP 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
 21-124 1.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   21 YPGVPQPSIPPYPGAPYPQPPFQPSPYSQPGYPqGTPSSYPQGGYPQDPypqAGyPQGPYPQAGYPQGPYPQGIYPQG-P 99
Cdd:PHA03247  2716 VSATPLPPGPAAARQASPALPAAPAPPAVPAGP-ATPGGPARPARPPTT---AG-PPAPAPPAAPAAGPPRRLTRPAVaS 2790

                           90       100
                   ....*....|....*....|....*....
gi 1910901021  100 YSQS----PFPPNPYGQPQAFPGQDPDSP 124
Cdd:PHA03247  2791 LSESreslPSPWDPADPPAAVLAPAAALP 2819
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-124 1.45e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGA---------PYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQagyPQGPYPQAGYPQGPYPQG-- 93
Cdd:PHA03247  2779 PPRRLTRPAVAslsesreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ---PTAPPPPPGPPPPSLPLGgs 2855

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1910901021   94 IYPQGPYSQSPfppnPYGQPQAFPGQDPDSP 124
Cdd:PHA03247  2856 VAPGGDVRRRP----PSRSPAAKPAAPARPP 2882
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 21-129 2.08e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 39.20  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  21 YPGVP---------------QPSIPPyPGAPYPQP------------------PFQPSPYSQPGYPQGTPSSYPQGGYPQ 67
Cdd:pfam15822  68 YPSIPltgpspgppapfppsGPSCPP-PGGPYPAPtvpgpgpigpyptpnmpfPELPRPYGAPTDPAAAAPSGPWGSMSS 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910901021  68 DPYPQAGYPQGPYPQAGYPQ-GPYPQGIYPQGPYSQSP-----FPPNPYGQPQAFPGQDPDSPQHGNY 129
Cdd:pfam15822 147 GPWAPGMGGQYPAPNMPYPSpGPYPAVPPPQSPGAAPPvpwgtVPPGPWGPPAPYPDPTGSYPMPGLY 214
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 25-124 2.21e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.05  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIP-------PYPGAPYPQPPFQPSPYS--QPGYP--QGTPS----------SYPQGGYPQD---PYPQAGYPQGPY 80
Cdd:COG5180   329 PRPGQPterpagvPEAASDAGQPPSAYPPAEeaVPGKPleQGAPRpgssggdgapFQPPNGAPQPglgRRGAPGPPMGAG 408

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1910901021  81 PQA-GYPQGPYPQGIYPQGPYSQSPFPPNPYGQP-QAFPGQDPDSP 124
Cdd:COG5180   409 DLVqAALDGGGRETASLGGAAGGAGQGPKADFVPgDAESVSGPAGL 454
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-125 2.24e-03

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 39.75  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPgaPYPQPPF----------QPSPYSQPGYPQgtPSSYPQGGYPQ---DPYPQAGYPQ-GPYPQAGYPQGPy 90
Cdd:NF033839  303 PQPEKKEVK--PEPETPKpevkpqlekpKPEVKPQPEKPK--PEVKPQLETPKpevKPQPEKPKPEvKPQPEKPKPEVK- 377

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1910901021  91 PQGIYPQGPYSQSPFPPNPYGQPQAFPGQDPDSPQ 125
Cdd:NF033839  378 PQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQ 412
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-109 2.41e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSsyPQGGYPQDPYPQAGYPQgPYPQAGYP-QGPYPQGIYPQ-GPYSQ 102
Cdd:PHA03247  2911 PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA--PTTDPAGAGEPSGAVPQ-PWLGALVPgRVAVPRFRVPQpAPSRE 2987


                   ....*..
gi 1910901021  103 SPFPPNP 109
Cdd:PHA03247  2988 APASSTP 2994
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 26-136 2.56e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGiyPQGPYSQSPF 105
Cdd:PRK07764  392 GAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPA--AAPSAQPAPA 469

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1910901021 106 PPNPyGQPQAFPGQDPDSPQHGNYHEEGPPS 136
Cdd:PRK07764  470 PAAA-PEPTAAPAPAPPAAPAPAAAPAAPAA 499
PHA03247 PHA03247
large tegument protein UL36; Provisional
 30-117 2.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   30 PPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYP----------------QAGYPQGPYPQAGYPQGPYPQG 93
Cdd:PHA03247  2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPerprddpapgrvsrprRARRLGRAAQASSPPQRPRRRA 2687

                           90       100
                   ....*....|....*....|....*
gi 1910901021   94 IYPQ-GPYSQSPFPPNPYGQPQAFP 117
Cdd:PHA03247  2688 ARPTvGSLTSLADPPPPPPTPEPAP 2712
KLF1_N cd21581
N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as ...
 25-127 3.30e-03

N-terminal domain of Kruppel-like Factor 1; Kruppel-like Factor 1 (KLF1, also known as Krueppel-like factor 1 or Erythroid Kruppel-like Factor/EKLF) was the first Kruppel-like factor discovered. It was found to be vitally important for embryonic erythropoiesis in promoting the switch from fetal hemoglobin (Hemoglobin F) to adult hemoglobin (Hemoglobin A) gene expression by binding to highly conserved CACCC domains. EKLF ablation in mouse embryos produces a lethal anemic phenotype, causing death by embryonic day 14, and natural mutations lead to beta+ thalassemia in humans. However, expression of embryonic hemoglobin and fetal hemoglobin genes is normal in EKLF-deficient mice, suggesting other factors may be involved. KLF1 functions as a transcriptional activator. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF1, which is related to the N-terminal domains of KLF2 and KLF4.


Pssm-ID: 409227 [Multi-domain]  Cd Length: 278  Bit Score: 38.87  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSPYS------QPGYPQGT----------PSSYPQGGYpqdpYPQAGYPQGPYPQAGYPQG 88
Cdd:cd21581   130 STGWAPPEPHHGYPDAFVGPALFPapanvdQFGFPQGGsvdrrgnlskSGSWDFGSY----YPQQHPSVVAFPDSRFGPL 205

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1910901021  89 PYPQGIYPQGPYsQSPFP-----PNPYGQPQAFPGQDPDSPQHG 127
Cdd:cd21581   206 SGPQALTPDPQH-YGYFQlfrhnAALFPDYAHSPGPGHLPLGQQ 248
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 34-94 3.43e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 39.42  E-value: 3.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1910901021  34 GAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYP---QGPYPQAGYPQGPYPQGI 94
Cdd:PRK13729  132 GEPVPQMPASPPGPEGEPQPGNTPVSFPPQGSVAVPPPTAFYPgngVTPPPQVTYQSVPVPNRI 195
PHA03378 PHA03378
EBNA-3B; Provisional
 33-136 3.90e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  33 PGAPYPqPPFQPSPYSQPGYPQGtPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGiyPQGPYSQSPFPPNPYGQ 112
Cdd:PHA03378  691 PGTMQP-PPRAPTPMRPPAAPPG-RAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAA--APGRARPPAAAPGRARP 766

                          90       100
                  ....*....|....*....|....
gi 1910901021 113 PQAFPGQDPDSPQhgnyhEEGPPS 136
Cdd:PHA03378  767 PAAAPGAPTPQPP-----PQAPPA 785
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 25-114 4.20e-03

pneumococcal surface protein PspC, LPXTG-anchored 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 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other 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.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 38.98  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPF-QPSPYSQPGYPQGTPSsypqggyPQDPYPQAgypqGPYPQAGYPQGPyPQGIYPQGPYSQS 103
Cdd:NF033839  290 KKPSAPKPGMQPSPQPEKkEVKPEPETPKPEVKPQ-------LEKPKPEV----KPQPEKPKPEVK-PQLETPKPEVKPQ 357

                          90
                  ....*....|.
gi 1910901021 104 PFPPNPYGQPQ 114
Cdd:NF033839  358 PEKPKPEVKPQ 368
PHA03378 PHA03378
EBNA-3B; Provisional
 31-112 4.64e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.28  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  31 PYPGAPYPQPPFQPSPySQPGYPQGTPS-SYPQGGYPQDPYPQAGYPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPNP 109
Cdd:PHA03378  736 PPAAAPGRARPPAAAP-GRARPPAAAPGrARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAA 814


                  ...
gi 1910901021 110 YGQ 112
Cdd:PHA03378  815 PGQ 817
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 25-122 5.60e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.81  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAP----YPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAgyPQGPYPQAGYPQGPYPQgiyPQGPY 100
Cdd:PRK07764  412 PAAAAPAAAAAPapaaAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA--QPAPAPAAAPEPTAAPA---PAPPA 486

                          90       100
                  ....*....|....*....|..
gi 1910901021 101 SQSPfPPNPYGQPQAFPGQDPD 122
Cdd:PRK07764  487 APAP-AAAPAAPAAPAAPAGAD 507
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 25-127 6.35e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 38.48  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  25 PQPSIPPYPGAPYPQPPFQPSP-------YSQPGY----------------PQGTPSSYPQGGYPQDPYPQAG------- 74
Cdd:pfam09770 118 PPASSLPQYQYASQQSQQPSKPvrtgyekYKEPEPipdlqvdaslwgvapkKAAAPAPAPQPAAQPASLPAPSrkmmsle 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1910901021  75 --------YPQGPYPQAGYPQGPYPQGIYPQGPYSQSPFPPNPYGQ--PQAFPGQDPDSPQHG 127
Cdd:pfam09770 198 eveaamraQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQqqPQQQPQQPQQHPGQG 260
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 9-127 6.95e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.43  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   9 VSGDNYPPPNPGYPGVPQPSIPPYPGAPYPQPPFQPSPYSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQGPYPQAGYPQG 88
Cdd:PRK07764  588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1910901021  89 PYPQGIYPQGPYS-----QSPFPPNPYGQPQAFPGQDPDSPQHG 127
Cdd:PRK07764  668 GWPAKAGGAAPAApppapAPAAPAAPAGAAPAQPAPAPAATPPA 711
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-73 7.26e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.77  E-value: 7.26e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1910901021    2 PHEKSFLVSG----DNYPPPNPGYPGVPQPSIPPYPgAPYPQPPFQPSPYSQPGYPQGtPSSYPQGGYPQDPYPQA 73
Cdd:PHA03247   389 RHAATPFARGpggdDQTRPAAPVPASVPTPAPTPVP-ASAPPPPATPLPSAEPGSDDG-PAPPPERQPPAPATEPA 462
PHA03247 PHA03247
large tegument protein UL36; Provisional
 25-145 7.65e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021   25 PQPSIPPYPGAPYP-----QPPFQ-----------------------PSPYSQPGYPQGTPS-SYPQGGY-PQDPYPQAG 74
Cdd:PHA03247  2504 PDPDAPPAPSRLAPailpdEPVGEpvhprmltwirgleelasddagdPPPPLPPAAPPAAPDrSVPPPRPaPRPSEPAVT 2583

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1910901021   75 ----YPQGPyPQAGYPQGPYPQGIYPQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPSYYDNQDFPA 145
Cdd:PHA03247  2584 srarRPDAP-PQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPA 2657
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 25-72 7.88e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 38.53  E-value: 7.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1910901021   25 PQPSIPPYPGAPYPQPPFQPSP-YSQPGYPQGTPSSYPQGGYPQDPYPQ 72
Cdd:PRK10263   794 PQQPVAPQPQYQQPQQPVAPQPqYQQPQQPVAPQPQYQQPQQPVAPQPQ 842
dnaA PRK14086
chromosomal replication initiator protein DnaA;
26-137 8.32e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 38.27  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910901021  26 QPSIPPYPGAPYPqPPFQPSP---YSQPGYPQGTPSSYPQGGYPQDPYPQAGYPQ-------GPYPQAGYPqgpyPQGIY 95
Cdd:PRK14086  169 QQRLGFPPRAPYA-SPASYAPeqeRDREPYDAGRPEYDQRRRDYDHPRPDWDRPRrdrtdrpEPPPGAGHV----HRGGP 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1910901021  96 PQGPYSQSPFPPNPYGQPQAFPGQDPDSPQHGNYHEEGPPSY 137
Cdd:PRK14086  244 GPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGEPTARLNPKY 285
 
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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