|
Name |
Accession |
Description |
Interval |
E-value |
| PH_ROCK |
cd01242 |
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is ... |
509-615 |
4.22e-57 |
|
Rho-associated coiled-coil containing protein kinase pleckstrin homology (PH) domain; ROCK is a serine/threonine kinase that binds GTP-Rho. It consists of a kinase domain, a coiled coil region and a PH domain. The ROCK PH domain is interrupted by a C1 domain. ROCK plays a role in cellular functions, such as contraction, adhesion, migration, and proliferation and in the regulation of apoptosis. There are two ROCK isoforms, ROCK1 and ROCK2. In ROCK2 the Rho Binding Domain (RBD) and the PH domain work together in membrane localization with RBD receiving the RhoA signal and the PH domain receiving the phospholipid signal. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269948 Cd Length: 110 Bit Score: 189.87 E-value: 4.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 509 SRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQCNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQI 588
Cdd:cd01242 1 SRLEGWLSLPNKQNIRRHGWKKQYVVVSSKKILFYNSEQDKANSNPILVLDIDKLFHVRSVTQGDVIRADAKEIPRIFQI 80
|
90 100 110
....*....|....*....|....*....|
gi 194387796 589 LYANEGESKKEQEFPVE---PVGEKSNYIC 615
Cdd:cd01242 81 LYANEGESSRPAEVTDTlsvSREEKPNTIL 110
|
|
| C1_ROCK2 |
cd20875 |
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ... |
608-678 |
7.16e-55 |
|
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410425 Cd Length: 71 Bit Score: 182.54 E-value: 7.16e-55
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387796 608 GEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYD 678
Cdd:cd20875 1 GEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVNYD 71
|
|
| C1_ROCK1 |
cd20874 |
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ... |
612-680 |
3.89e-47 |
|
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410424 Cd Length: 69 Bit Score: 160.95 E-value: 3.89e-47
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387796 612 NYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDIS 680
Cdd:cd20874 1 NFLPHKGHEFIPTLYHFPANCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDMITPCKVNYDVT 69
|
|
| C1_ROCK |
cd20813 |
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil ... |
612-676 |
1.54e-39 |
|
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil containing protein kinase (ROCK) family; ROCK is a serine/threonine protein kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410363 Cd Length: 65 Bit Score: 139.71 E-value: 1.54e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194387796 612 NYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVY 676
Cdd:cd20813 1 GTISHKGHEFVEITFHMPTTCDVCHKPLWHLFKPPPALECKRCRMKIHKDHVDKEEYFIPPCKVN 65
|
|
| ROCK_SBD |
cd22250 |
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; ... |
214-294 |
4.17e-28 |
|
Shroom-binding domain found in Rho-associated coiled-coil containing protein kinase; Rho-associated coiled-coil containing protein kinase (ROCK) is a serine/threonine kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated protein kinase or simply as Rho kinase. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Rho-associated protein kinase 1 (ROCK1) is also called renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase 1, ROCK-I, p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient in ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. Rho-associated protein kinase 2 (ROCK2), also called Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, ROCK-II, or p164 ROCK-2, is more prominent in brain and skeletal muscle. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK subfamily proteins contain an N-terminal extension, a catalytic kinase domain, a coiled-coil (CC) region encompassing a Rho-binding domain (RBD), and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via proteolytic cleavage, binding of lipids to the PH domain, or binding of GTP-bound RhoA to the CC region. More recently, the Shroom family of proteins have been identified as an additional regulator of ROCK. This model corresponds to the Shroom-binding domain (SBD) of ROCK, which forms a parallel coiled coil with the Shroom domain 2 (SD2) of Shroom.
Pssm-ID: 409019 [Multi-domain] Cd Length: 75 Bit Score: 107.73 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 214 DGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKlgkelqQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQ 293
Cdd:cd22250 1 DLQMKELQDQLEAEQYFSTLYKTQVKELKEELEEKTR------QIKQELEDERESLSAQLELALAKADSEQLARSIAEEQ 74
|
.
gi 194387796 294 Y 294
Cdd:cd22250 75 I 75
|
|
| Rho_Binding |
pfam08912 |
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding ... |
337-404 |
2.16e-20 |
|
Rho Binding; Rho Binding Domain is responsible for the recognition and binding of Rho binding domain-containing proteins (such as ROCK) to Rho, resulting in activation of the GTPase which in turn modulates the phosphorylation of various signalling proteins. This domain is within an amphipathic alpha-helical coiled-coil and interacts with Rho through predominantly hydrophobic interactions.
Pssm-ID: 462630 [Multi-domain] Cd Length: 68 Bit Score: 85.40 E-value: 2.16e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 337 TSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 404
Cdd:pfam08912 1 TKDVENLAKEKEELNNKLKEQQEELEKAKEEEEEIEKLKASYEKQLNTERTLKTQAVNKLAEIMNRKD 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-522 |
2.23e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 133 INELLKQKDVLNEDVRN----LTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRK 208
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 209 ERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEitltkADSEQLARs 288
Cdd:COG1196 275 ELEELELELEEAQAEEYELL-------AELARLEQDIARLEERRRELEERLEELEEELAELEEELE-----ELEEELEE- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 289 iAEEQYSDLEKEKIMKELEIKEmmarHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEE 368
Cdd:COG1196 342 -LEEELEEAEEELEEAEAELAE----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 369 ISAAAIKAQFEKQLLTERTLKTQAVNKLAEImnrkepvkrgndtdvRRKEKENRKLHMELKSEREKLTQQMIKYQKELNE 448
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEA---------------AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387796 449 MQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNN 522
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
|
| C1 |
smart00109 |
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ... |
619-665 |
7.23e-14 |
|
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.
Pssm-ID: 197519 Cd Length: 50 Bit Score: 66.34 E-value: 7.23e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDK 665
Cdd:smart00109 1 HKHVFRTFTKPTFCCVCRKSIWGSFK--QGLRCSECKVKCHKKCADK 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-404 |
3.21e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 132 KINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQ 211
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 212 DADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAE 291
Cdd:COG1196 313 ELEERLEELEEELAELE-------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 292 EQYSDLEKEKIMKELEIKEMMARHKQELTEkdatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISA 371
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270
....*....|....*....|....*....|...
gi 194387796 372 AAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 404
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-484 |
3.79e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 199 LEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLT 278
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 279 KADSEQLARSIAEEQYSDLEK--EKIMKELE-IKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLK 355
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAqiEQLKEELKaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 356 DVQEQLSRLKDEEISAAAIKAQFEKQLlterTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKL 435
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESEL----EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 194387796 436 TQ---QMIKYQKELNEMQAQIAEESQIRIELQMTLDSK-DSDIEQLRSQLQAL 484
Cdd:TIGR02168 925 AQlelRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKiEDDEEEARRRLKRL 977
|
|
| C1 |
cd00029 |
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ... |
619-673 |
5.48e-13 |
|
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.
Pssm-ID: 410341 Cd Length: 50 Bit Score: 63.69 E-value: 5.48e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDKkeeIIAPC 673
Cdd:cd00029 1 HRFVPTTFSSPTFCDVCGKLIWGLFK--QGLKCSDCGLVCHKKCLDK---APSPC 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-401 |
5.83e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 25 LEKRQLQ----ERFTDLEKEKSNMEIDmtyqlkVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAmkemEKKLLE 100
Cdd:TIGR02168 202 LKSLERQaekaERYKELKAELRELELA------LLVLRLEELREELEELQEELKEAEEELEELTAELQEL----EEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 101 ERTLKQKVENLLLEAEKRcslldcdLKQSQQKINELLKQKDVLNEDVRNLTLKIEQetqkrclTQNDLKMQTQQVNTLKM 180
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERLANLERQLEE-------LEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 181 SEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEaeqyfstlykTQVRELKEECEEKTKLGKELQQKKQ 260
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 261 ELqderdslaaqleitltkadsEQLARSIAEEQYSDLEKEKIMKELEIKEmmarHKQELTEKDATIASLEETNRTLTSDV 340
Cdd:TIGR02168 408 RL--------------------ERLEDRRERLQQEIEELLKKLEEAELKE----LQAELEELEEELEELQEELERLEEAL 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194387796 341 ANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFE------KQLLTERTLKTQAVNKLAEIMN 401
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELIS 530
|
|
| PH_MRCK |
cd01243 |
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK ... |
512-588 |
6.59e-12 |
|
MRCK (myotonic dystrophy-related Cdc42-binding kinase) pleckstrin homology (PH) domain; MRCK is thought to be coincidence detector of signaling by Cdc42 and phosphoinositides. It has been shown to promote cytoskeletal reorganization, which affects many biological processes. There are 2 members of this family: MRCKalpha and MRCKbeta. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. The MRCK PH domain is responsible for its targeting to cell to cell junctions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 269949 Cd Length: 135 Bit Score: 63.47 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 512 EGWLSLPVRNNTKKfGWVKKYVIVSSKKILFYDSEQDKEQ---CNPYMVLDI-DKLFHVRPVTQTDVYRADAKEIPRIFQ 587
Cdd:cd01243 15 EGYVRVPKPGGVKK-GWQRQFAVVCDFKLFLFDISEDKASqpsQVASQVLDMrDEEFSVSSVLASDVIHANKKDIPCIFR 93
|
.
gi 194387796 588 I 588
Cdd:cd01243 94 V 94
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-484 |
3.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIdmtyQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKS 88
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 EAMKEMEKKLLEERTLKQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQ 165
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 NDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEEC 245
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EEKTKLGKELQQKKQELQDERDSLAAQLE----------ITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARH 315
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEAdyegflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 316 KQELTEKDATIASLEETNRtltSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNK 395
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKA---GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 396 LAEIMNRKEPVKRGNDTDV---------------RRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIR 460
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREvtlegeggsaggsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500
....*....|....*....|....
gi 194387796 461 IELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAE 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
57-402 |
4.88e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 57 QSLEQEEAEHKATKARLADKnkiyesiEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINEL 136
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEK-------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 137 LKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQ 216
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 217 MKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSD 296
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 297 LEKEKIMKE---LEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEE-LNNKLKDVQEQLSRLKDE----- 367
Cdd:TIGR02168 906 LESKRSELRrelEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKikelg 985
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 194387796 368 EISAAAIkAQFEKQ------LLTERTLKTQAVNKLAEIMNR 402
Cdd:TIGR02168 986 PVNLAAI-EEYEELkerydfLTAQKEDLTEAKETLEEAIEE 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-484 |
5.69e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 127 KQSQQKINE----LLKQKDVLNEDVRNLtlkieqetqkrcltqNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMN-LEK 201
Cdd:TIGR02168 175 KETERKLERtrenLDRLEDILNELERQL---------------KSLERQAEKAERYKELKAELRELELALLVLRLEeLRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 202 QNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQderdslaaqLEITLTKAD 281
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---------QQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 282 SEQLARSIAEEQYSDLEKEKimKELEIKEMMARHKQELTEKDATIASLEEtnrtltsDVANLANEKEELNNKLKDVQEQL 361
Cdd:TIGR02168 311 LANLERQLEELEAQLEELES--KLDELAEELAELEEKLEELKEELESLEA-------ELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 362 SRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRgndtdvRRKEKENRKLHMELKSEREKLTQQmik 441
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK------KLEEAELKELQAELEELEEELEEL--- 452
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 194387796 442 yQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:TIGR02168 453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-484 |
1.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQ---LKVIQQSLEQEEAEHKATKARLADKNKIYESIEE 85
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 86 AKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSlldcDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQ 165
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 NDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYfSTLYKTQVRELKEEC 245
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-ELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EE---------KTKLGKELQQKK--------------------------QELQDERDSLAAQLEITLTKADSEQLARSIA 290
Cdd:COG1196 500 EAdyegflegvKAALLLAGLRGLagavavligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 291 EEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNnKLKDVQEQLSRLKDEEIS 370
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV-TLAGRLREVTLEGEGGSA 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 371 AAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEpvKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQ 450
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEE--LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 194387796 451 AQIAEESQIRIELQMTLDSKDSD---------IEQLRSQLQAL 484
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPpdleelereLERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-375 |
2.69e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKV-------ELEKRQLQERFTDLEKEKSNMEIDMTyQLKVIQQSLEQEEAEHKATKARLADKNKIYE 81
Cdd:TIGR02168 689 LEEKIAELEKALAELrkeleelEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 82 SIEEAKSEAMKEMEKKLLEertLKQKVENLLLEaekrcslldcdLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKR 161
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEE---LEAQIEQLKEE-----------LKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 162 CLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVREL 241
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 242 KEECEEKTKLGKELQQKKQELQDERDSLAAQLeitltkadseqlarsiaEEQYSDLEKEKIMKELEIKEMMARHKQELTE 321
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERL-----------------SEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 322 KDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKD--EEISAAAIK 375
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEaiEEIDREARE 1032
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-353 |
1.24e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 114 EAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQEnnhLM 193
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 194 EMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQL 273
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 274 EitltkadseqlarsIAEEQYSDLEKEKIMKEleikEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 353
Cdd:COG4942 181 A--------------ELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-484 |
1.83e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 17 KILLAKVEL-EKRQLQERFTdleKEKSNMEiDMTYQLKVIQQSLEQEEAEHKATKARLADKNKiyesieeAKSEAMKEME 95
Cdd:pfam15921 350 QLVLANSELtEARTERDQFS---QESGNLD-DQLQKLLADLHKREKELSLEKEQNKRLWDRDT-------GNSITIDHLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 96 KKLLEERTLKQKVENLLLEAEKRCSlldcdlKQSQQKINELLKQKDVLnEDVRNLTLKIEQETQkrcLTQNDLKMQTQQV 175
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSECQ------GQMERQMAAIQGKNESL-EKVSSLTAQLESTKE---MLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 176 NTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQdQLEAEQYFSTLYKTQVRELKEECEEKTKLGKEL 255
Cdd:pfam15921 489 MTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 256 QQKKQEL-----QDERDSLAAQLEitltkadseqlarsiaeeqYSDLEKEKIMKELEIKEMmarhKQELTEKDATIASLE 330
Cdd:pfam15921 568 RQQIENMtqlvgQHGRTAGAMQVE-------------------KAQLEKEINDRRLELQEF----KILKDKKDAKIRELE 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 331 ETNRTLTSDVANLANEKEELNNKLKDVQEQlsrlkdeeisaaaikaqfEKQLLTERTLKTQAVNKLAEimnRKEPVKRGN 410
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKQE------------------RDQLLNEVKTSRNELNSLSE---DYEVLKRNF 683
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387796 411 DTDVRRKEKENRKLHMELKSEREKLTQQmikyQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQT----RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL 753
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
10-490 |
2.00e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.34 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 10 EEDLKNGKILLAKVELEKRQLQERFTDLEKEKSnmeidmtyqlkVIQQSLEQEE---AEHKATKARLADKNKIYESI--- 83
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKN-----------ALQEQLQAETelcAEAEEMRARLAARKQELEEIlhe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 84 -------EEAKSEAM-----------KEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNE 145
Cdd:pfam01576 80 lesrleeEEERSQQLqnekkkmqqhiQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 146 DVRNLTLKIEQETQKrclTQNDLKMQTQQVNTLKMSEKQLKQEnnhlmemkmnlEKQNAELRKERQDADGQMKELQDQLE 225
Cdd:pfam01576 160 RISEFTSNLAEEEEK---AKSLSKLKNKHEAMISDLEERLKKE-----------EKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 226 AEQyfstlykTQVRELKeeceektklgKELQQKKQELQDerdslaaqleiTLTKADSEQLARSIAEEQYSDLEKE--KIM 303
Cdd:pfam01576 226 ELQ-------AQIAELR----------AQLAKKEEELQA-----------ALARLEEETAQKNNALKKIRELEAQisELQ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 304 KELEiKEMMARHKQELTEKDatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAaaikaqFEKQLL 383
Cdd:pfam01576 278 EDLE-SERAARNKAEKQRRD--LGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRS------HEAQLQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 384 TERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKS----------EREKLTQQMIKYQKELNEMQAQI 453
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTlqqakqdsehKRKKLEGQLQELQARLSESERQR 428
|
490 500 510
....*....|....*....|....*....|....*..
gi 194387796 454 AEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDS 490
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-484 |
2.62e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKeksnmeidmtyQLKVIQQSLEQEEAEHKATKARLADKNKIYESIE---E 85
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLER-----------QLEELEAQLEELESKLDELAEELAELEEKLEELKeelE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 86 AKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLtlKIEQETQKRCLTQ 165
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL--QQEIEELLKKLEE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 NDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstlyktqVRELKEEC 245
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-----------LERLQENL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EEKTKLGKELQQKKQELQDERDSLAAQLEIT--LTKADSEQLARSIAEEQYSDLEK-EKIMKELEIKEMMARHKQELT-E 321
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDegYEAAIEAALGGRLQAVVVENLNAaKKAIAFLKQNELGRVTFLPLDsI 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 322 KDATIASLEETNRTLTSDVANLANEKEELNNKLKDV-----------------QEQLSRLKDEE---------------- 368
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddldnaLELAKKLRPGYrivtldgdlvrpggvi 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 369 ---------------ISAAAIKAQFEKQLLTERTLKtQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELK---S 430
Cdd:TIGR02168 662 tggsaktnssilerrREIEELEEKIEELEEKIAELE-KALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleA 740
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 194387796 431 EREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-407 |
2.76e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 102 RTLKQKVENLLLeaekrcSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcLTQNDLKMQ---------T 172
Cdd:TIGR02168 216 KELKAELRELEL------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK--LEELRLEVSeleeeieelQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 173 QQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLG 252
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 253 KELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEmmARHKQELTEKDATIASLEET 332
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE--LLKKLEEAELKELQAELEEL 445
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194387796 333 NRtltsdvanlanEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVK 407
Cdd:TIGR02168 446 EE-----------ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
209-484 |
8.35e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 8.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 209 ERQDADGQMKELQDQLEAEQYFSTLYKT-QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTK-------- 279
Cdd:COG3206 62 EPQSSDVLLSGLSSLSASDSPLETQIEIlKSRPVLERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKgsnvieis 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 280 --ADSEQLARSIAE-------EQYSDLEKEKIMKELE-IKEMMARHKQELTEKDATIASLEETNrtltsDVANLANEKEE 349
Cdd:COG3206 142 ytSPDPELAAAVANalaeaylEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 350 LNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNklaeimnrkepvkrgnDTDVRRKEKENRKLHMELK 429
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------SPVIQQLRAQLAELEAELA 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 430 SEREKLTQQMIKYQkelnEMQAQIAE-ESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:COG3206 281 ELSARYTPNHPDVI----ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASL 332
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-275 |
1.09e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIdmtyQLKVIQQSLEQEEAEHKATKARLAD---KNKIYESIEE 85
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ----QKQILRERLANLERQLEELEAQLEElesKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 86 AKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNL------------TLK 153
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLearlerledrreRLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 154 IEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstl 233
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS------- 493
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 194387796 234 yktqVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEI 275
Cdd:TIGR02168 494 ----LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-367 |
1.16e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 16 GKILLAKVELEK-RQLQERFTDLEKEKSNmeidmtyqlkvIQQSLEQEEAEHKATKARLADKnkiyesiEEAKSEAMKEM 94
Cdd:TIGR02169 664 GGILFSRSEPAElQRLRERLEGLKRELSS-----------LQSELRRIENRLDELSQELSDA-------SRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 95 EKKLLEERTLKQKVENLlleaEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQetQKRCLTQNDLKMQTQQ 174
Cdd:TIGR02169 726 EQLEQEEEKLKERLEEL----EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 175 VNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKE 254
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 255 LQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKD---------AT 325
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEeelsledvqAE 959
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 194387796 326 IASLEETNRTLtSDVANLA-NEKEELNNKLKDVQEQLSRLKDE 367
Cdd:TIGR02169 960 LQRVEEEIRAL-EPVNMLAiQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| C1_Myosin-IX |
cd20818 |
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ... |
616-660 |
1.68e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410368 Cd Length: 56 Bit Score: 51.15 E-value: 1.68e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 660
Cdd:cd20818 1 HNGHKFATVQFNIPTYCEVCNSFIWLMEK---GLVCQVCKFTCHK 42
|
|
| C1_p190RhoGEF-like |
cd20815 |
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide ... |
617-673 |
1.90e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in the 190 kDa guanine nucleotide exchange factor (p190RhoGEF)-like family; The p190RhoGEF-like protein family includes p190RhoGEF, Rho guanine nucleotide exchange factor 2 (ARHGEF2), A-kinase anchor protein 13 (AKAP-13) and similar proteins. p190RhoGEF is a brain-enriched, RhoA-specific guanine nucleotide exchange factor that regulates signaling pathways downstream of integrins and growth factor receptors. It is involved in axonal branching, synapse formation and dendritic morphogenesis, as well as in focal adhesion formation, cell motility and B-lymphocytes activation. ARHGEF2 acts as a guanine nucleotide exchange factor (GEF) that activates Rho-GTPases by promoting the exchange of GDP for GTP. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. AKAP-13 is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. It activates RhoA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Members of this family share a common domain architecture containing C1, RhoGEF or Dbl-homologous (DH), and Pleckstrin Homology (PH) domains. Some members may contain additional domains such as the DUF5401 domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410365 Cd Length: 54 Bit Score: 50.88 E-value: 1.90e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387796 617 KGHEFIPTLYHFPTNCEACMKPLwhmfKPPPALECRRCHIKCH----KDHmdkkeeiIAPC 673
Cdd:cd20815 2 NTHQFVPVSFSNSTKCDVCSKPL----TNKPALQCENCSVNVHdsscKDQ-------LADC 51
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-482 |
2.36e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 26 EKRQLQERFTDLEKEKSNMEIDMT------YQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLL 99
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDkiknklLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 100 EERTLKQKVENLLLEAEKRCSLLD---CDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRclTQNDLKMQTQQVN 176
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE--LKSELKNQEKKLE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 177 TLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQL-----EAEQYFSTLY--KTQVRELKEECEEKT 249
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkkENQSYKQEIKnlESQINDLESKIQNQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 250 KLGKELQQKKQELQDERDSLaaQLEITLTKADSEQLARSIaeeqySDLEKEKIMKELEIKEMMARHKQELTEKDATIASL 329
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELL--EKEIERLKETIIKNNSEI-----KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 330 EETNRTL----------TSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQL-------------LTER 386
Cdd:TIGR04523 478 NKIKQNLeqkqkelkskEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdledelnkddfeLKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 387 TLKTQAVNKLAEIMNRKEpvkrgNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQI--AEESQIRIELQ 464
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQ-----TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELekAKKENEKLSSI 632
|
490
....*....|....*....
gi 194387796 465 -MTLDSKDSDIEQLRSQLQ 482
Cdd:TIGR04523 633 iKNIKSKKNKLKQEVKQIK 651
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
87-449 |
2.51e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 87 KSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQK--INELLKQKDVLNEDVRNLTLKIEQETQKRCLT 164
Cdd:pfam02463 664 VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKeeLKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 165 QNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQyfstlyktQVRELKEE 244
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE--------EELKEEAE 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 245 CEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDA 324
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 325 TIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIS--AAAIKAQFEKQLLTERTLKTQAVNKLAEIMNR 402
Cdd:pfam02463 896 KEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLleEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 194387796 403 KEPVKRgndtDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEM 449
Cdd:pfam02463 976 NLMAIE----EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| C1_PDZD8 |
cd20825 |
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ... |
616-665 |
4.36e-08 |
|
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410375 Cd Length: 55 Bit Score: 49.97 E-value: 4.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFkpppALECRRCHIKCHKDHMDK 665
Cdd:cd20825 1 EGKHDFVLTQFQNATYCDFCKKKIWLKE----AFQCRLCGMICHKKCLDK 46
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
25-348 |
9.97e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 25 LEKRQLQERFTDLEKEKSNMEIDMtyQLKVIQQSLEQEEAEhKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTL 104
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEE--KAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 105 KQ---KVENLLLEAEKRCSLLdcDLKQSQQKINELLKQKdvlNEDVRNltLKIEQETQKRcltqndlKMQTQQVNTLKMS 181
Cdd:pfam17380 361 ELeriRQEEIAMEISRMRELE--RLQMERQQKNERVRQE---LEAARK--VKILEEERQR-------KIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 182 EKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQlEAEQYFSTLYKTQVRELKEECEEKTK--LGKELQQKK 259
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRkiLEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 260 QELQDERDslaaqlEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQ--ELTEKDATIASLEETNRTLT 337
Cdd:pfam17380 506 QAMIEEER------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmrKATEERSRLEAMEREREMMR 579
|
330
....*....|.
gi 194387796 338 SDVANLANEKE 348
Cdd:pfam17380 580 QIVESEKARAE 590
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
78-457 |
1.06e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 78 KIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQE 157
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 158 TQKRCLT---QNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLY 234
Cdd:pfam02463 222 EEEYLLYldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 235 KTQVRELKEECEEKTKLGKELQQKKQElqderdslaaqleitltKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMAR 314
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEK-----------------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 315 HKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVN 394
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387796 395 KLAEimnrkepvkrGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEES 457
Cdd:pfam02463 445 KLTE----------EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
290-536 |
1.63e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 290 AEEQYSDLEKEKImkelEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEI 369
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 370 SA----AAIKAQFEKQLlteRTL-KTQAVNKLAEIMNRKEPVK---------------RGNDTDVRRKEKENRKLHMELK 429
Cdd:COG4942 94 ELraelEAQKEELAELL---RALyRLGRQPPLALLLSPEDFLDavrrlqylkylaparREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 430 SEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHiGLDSSSIGSGPGDAEADDGFPES 509
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAAAERTPAAGFA 249
|
250 260
....*....|....*....|....*...
gi 194387796 510 RLEGWLSLPVRNN-TKKFGWVKKYVIVS 536
Cdd:COG4942 250 ALKGKLPWPVSGRvVRRFGERDGGGGRN 277
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
27-486 |
1.84e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 27 KRQLQERFTDLEKEKS---NMEIDMTYQLKVIQQSLEQEEAEHKATKARLAD-----KNKIYE----------SIEEAKS 88
Cdd:pfam15921 144 RNQLQNTVHELEAAKClkeDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfeeasGKKIYEhdsmstmhfrSLGSAIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 EAMKEMEKKL--LEERT--LKQKVENLLLEAEKRCSLLdcdLKQSQQKINELLKQKDVlneDVRNLTlkiEQETQKRCLT 164
Cdd:pfam15921 224 KILRELDTEIsyLKGRIfpVEDQLEALKSESQNKIELL---LQQHQDRIEQLISEHEV---EITGLT---EKASSARSQA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 165 QNdlkMQTQqvntLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEE 244
Cdd:pfam15921 295 NS---IQSQ----LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 245 -CEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADS--------EQLARSIAEEQYSDLEKEKIMKEL------EIK 309
Cdd:pfam15921 368 fSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitiDHLRRELDDRNMEVQRLEALLKAMksecqgQME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 310 EMMA--RHKQELTEKDATI-ASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKqLLTER 386
Cdd:pfam15921 448 RQMAaiQGKNESLEKVSSLtAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK-LRSRV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 387 TLKTQAVNKLAEIMNRKEPVKRGNDTdVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAE-ESQI---RIE 462
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQlEKEIndrRLE 605
|
490 500
....*....|....*....|....*..
gi 194387796 463 LQ---MTLDSKDSDIEQLRSQLQALHI 486
Cdd:pfam15921 606 LQefkILKDKKDAKIRELEARVSDLEL 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-445 |
2.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 237 QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIA--EEQYSDLEKEKimkeleikemmar 314
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAelEAELERLDASS------------- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 315 hkQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERtlktqavn 394
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER-------- 754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 194387796 395 klaeimnRKEPVKRGNDTDVRRK-EKENRKLHMELKSEREKLTQQMIKYQKE 445
Cdd:COG4913 755 -------FAAALGDAVERELRENlEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-484 |
3.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 204 AELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLgKELQQKKQELqdERDSLAAQLEITLTKADSE 283
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 284 QLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDA----TIASLEETNRTLTSDVANLANEKEELNNKLKDVQE 359
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 360 QLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAE-------IMNRKEPVKRGNDTDVRRKEKENRKLHM------ 426
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAElkeeledLRAELEEVDKEFAETRDELKDYREKLEKlkrein 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 427 ELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-288 |
4.43e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 56 QQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKklLEERTlkQKVENLLLEAEKRCSLLDCDLKQSQQKINE 135
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--LERRI--AALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 136 LLK----QKDVLNEDVRNLTLKIEQETQKRCLTQND-------LKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNA 204
Cdd:COG4942 95 LRAeleaQKEELAELLRALYRLGRQPPLALLLSPEDfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 205 ELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQ 284
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQ-------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....
gi 194387796 285 LARS 288
Cdd:COG4942 248 FAAL 251
|
|
| C1_1 |
pfam00130 |
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ... |
619-661 |
4.46e-07 |
|
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.
Pssm-ID: 395079 Cd Length: 53 Bit Score: 47.05 E-value: 4.46e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKD 661
Cdd:pfam00130 1 HHFVHRNFKQPTFCDHCGEFLWGLGKQ--GLKCSWCKLNVHKR 41
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
190-399 |
5.45e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 190 NHLME--MKMNLEKQNAELRKERQDADGQMKELQDQL-EAEQYFSTlYKTQ--VRELKEECEEKTKLGKELQQKKQELQD 264
Cdd:COG3206 155 NALAEayLEQNLELRREEARKALEFLEEQLPELRKELeEAEAALEE-FRQKngLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 265 ERDSLAAQLEI--TLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQE---LTEKDATIASLEETNRTLTSD 339
Cdd:COG3206 234 ELAEAEARLAAlrAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387796 340 V-ANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQF---EKQLLTERTLKTQAVNKLAEI 399
Cdd:COG3206 314 IlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrrlEREVEVARELYESLLQRLEEA 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-464 |
5.91e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 11 EDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKiyESIEEAKSEA 90
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA--EAAEKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 91 MKEME--KKLLEER-----------TLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQE 157
Cdd:PTZ00121 1377 KKKADaaKKKAEEKkkadeakkkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 158 TQKRCLTQ--------NDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLE--KQNAELRK--ERQDADgQMKELQDQLE 225
Cdd:PTZ00121 1457 KKAEEAKKkaeeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKaeEAKKAD-EAKKAEEAKK 1535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 226 AEQYFSTLYKTQVRELKEECE-EKTKLGKELQQKKQELQDERDSL-AAQLEITLTKADSEQLARSIAEEQYSDLEKEKIM 303
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAEEDKNMALrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 304 KELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVanlanEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLL 383
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-----KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 384 TERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSERE---KLTQQMIKYQKELNEMQAQIAEESQIR 460
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
....
gi 194387796 461 IELQ 464
Cdd:PTZ00121 1771 EEIR 1774
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
187-472 |
7.47e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 187 QENNHLME----MKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQEL 262
Cdd:pfam07888 41 QERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAE-------LKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 263 QDERDSLAAQleitltKADSEQLARSIaEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDAtiaslEETnrtltsdvan 342
Cdd:pfam07888 114 SEEKDALLAQ------RAAHEARIREL-EEDIKTLTQRVLERETELERMKERAKKAGAQRKE-----EEA---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 343 lanEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLaeimnrkepvkrgndTDVRRKEKENR 422
Cdd:pfam07888 172 ---ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---------------TTAHRKEAENE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 423 KLHMELKSEREKLT---QQMIKYQKELNEMQAQ----IAEESQIRIEL-QMTLDSKDS 472
Cdd:pfam07888 234 ALLEELRSLQERLNaseRKVEGLGEELSSMAAQrdrtQAELHQARLQAaQLTLQLADA 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-382 |
7.51e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 198 NLEKQNAELRKERQDADGQMKELQDQLEA--EQYFSTlyKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEI 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEElnEEYNEL--QAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 276 TLTKADSEQL---ARSIAE--EQYSDLEKekIMKELeiKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEEL 350
Cdd:COG3883 98 SGGSVSYLDVllgSESFSDflDRLSALSK--IADAD--ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|..
gi 194387796 351 NNKLKDVQEQLSRLKDEEISAAAIKAQFEKQL 382
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
26-480 |
1.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 26 EKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQeeAEHKATKARLADKNKIYESIEEAKsEAMKEMEKKLLEErtLK 105
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADE--AK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 106 QKVEnlllEAEKRcslldcdlKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQL 185
Cdd:PTZ00121 1309 KKAE----EAKKA--------DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 186 KQENNHLMemKMNLEKQNAELRKERQDADGQMKELQDQLEAEqyfstlyKTQVRELKEECEEKTKlGKELQQKKQELQDE 265
Cdd:PTZ00121 1377 KKKADAAK--KKAEEKKKADEAKKKAEEDKKKADELKKAAAA-------KKKADEAKKKAEEKKK-ADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 266 RDSlaaqleitltKADSEQLARsiAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKdatiasLEETNRTltsdvANLAN 345
Cdd:PTZ00121 1447 DEA----------KKKAEEAKK--AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK------AEEAKKK-----ADEAK 1503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 346 EKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKlAEIMNRKEPVKRGNDtdvRRKEKENRKLH 425
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK-AEELKKAEEKKKAEE---AKKAEEDKNMA 1579
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387796 426 M----ELKSEREKLTQQMIKYQKELNEM---QAQIAEESQIRIELQMTLDSKDSDIEQLRSQ 480
Cdd:PTZ00121 1580 LrkaeEAKKAEEARIEEVMKLYEEEKKMkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
123-332 |
1.23e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 123 DCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrcltQNDLKMQtqqvntLKMSEKQLKQENNHLMEMKMNLEKQ 202
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAE------LEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 203 NAELRKE-----RQDADGQM-------KELQDQLEAEQYFSTLYKTQ---VRELKEECEEKTKLGKELQQKKQELQDERD 267
Cdd:COG3883 85 REELGERaralyRSGGSVSYldvllgsESFSDFLDRLSALSKIADADadlLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 268 SLAAQL-EITLTKADSEQLARSIAEEQySDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEET 332
Cdd:COG3883 165 ELEAAKaELEAQQAEQEALLAQLSAEE-AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
57-484 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 57 QSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEK--KLLEERTLKQKVENLLLEAEKRCSLLDcDLKQSQQKIN 134
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 135 ELLKQKDVLNEDVRNLTLKIEQETQKRCL-TQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDA 213
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 214 dgqmkELQDQLEAEQYFSTLYKTQVrelkeeceEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQ 293
Cdd:COG4717 240 -----ALEERLKEARLLLLIAAALL--------ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 294 YSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELnnKLKDVQEQLSRLkdeeisAAA 373
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAAL------LAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 374 IKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKlhmELKSEREKLTQQMIKYQKELNEMQAQI 453
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEELEEELEELREEL 455
|
410 420 430
....*....|....*....|....*....|...
gi 194387796 454 AE-ESQIR-IELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:COG4717 456 AElEAELEqLEEDGELAELLQELEELKAELREL 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-380 |
1.40e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 174 QVNTLKMSEKQLKQENNHLMEmkmnLEKQNAELRKERQDADGQMKELQDQLEAEQyfsTLYKTQVRELKEECEEKTKLGK 253
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAE----LEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 254 ELQQKKQELQDERDSLAAQL------------EITLTKADSEQLARSIA-EEQYSDLEKEKIMKELEIKEMMARHKQELT 320
Cdd:COG4942 91 EIAELRAELEAQKEELAELLralyrlgrqpplALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387796 321 EKDATIASLEETNRTLTSDVANLANEKEELNNKL-KDVQEQLSRLKDEEISAAAIKAQFEK 380
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-317 |
1.53e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 20 LAKVELEKRQLqERFTDLEKEKSNMEI--------DMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAM 91
Cdd:TIGR02169 200 LERLRREREKA-ERYQALLKEKREYEGyellkekeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 92 KEMEKKLLEE-RTLKQKVENLLLE---AEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQND 167
Cdd:TIGR02169 279 KKIKDLGEEEqLRVKEKIGELEAEiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 168 LKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQyfstlykTQVRELKEECEE 247
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS-------EELADLNAAIAG 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 248 KTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQ 317
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-482 |
3.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 22 KVELEKRQLQERFTDLEKEKSNMEidmtyQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEE 101
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELE-----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 102 RTLKQKVE---------NLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQ------ETQKRCLTQN 166
Cdd:PRK03918 286 KELKEKAEeyiklsefyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 167 DLKMQTQQVNTLKMSEK-----QLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEA--------------- 226
Cdd:PRK03918 366 EAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrel 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 227 -EQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARsiAEEQYSDLEKEKIMKE 305
Cdd:PRK03918 446 tEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE--LEEKLKKYNLEELEKK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 306 LEIKEMMarhKQELTEKDATIASLEETnrtlTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAaikaqFEKQLLTE 385
Cdd:PRK03918 524 AEEYEKL---KEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDELEEELAELLKELEELG-----FESVEELE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 386 RTLKtqavnKLAEIMNRKEPVKrGNDTDVRRKEKENRKLHMELKSEREKLTQ---QMIKYQKELNEMQAQIAEESQIRI- 461
Cdd:PRK03918 592 ERLK-----ELEPFYNEYLELK-DAEKELEREEKELKKLEEELDKAFEELAEtekRLEELRKELEELEKKYSEEEYEELr 665
|
490 500
....*....|....*....|....*
gi 194387796 462 ----ELQMTLDSKDSDIEQLRSQLQ 482
Cdd:PRK03918 666 eeylELSRELAGLRAELEELEKRRE 690
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-484 |
4.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEiDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKS 88
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 EAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTlkieQETQKRCLTQNDL 168
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT----EEHRKELLEEYTA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 169 KMQTQQvNTLKMSEKQLKQENNHLMEMKMNLEKQnAELRKERQDADgQMKELQDQLEAEQyfstlyktqvrelKEECEEK 248
Cdd:PRK03918 460 ELKRIE-KELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAE-QLKELEEKLKKYN-------------LEELEKK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 249 TKLGKELQQKKQELQDERDSLAAQLeitltkadseqlarsiaeEQYSDLEKEKIMKELEIKEMMARHKQELTE-KDATIA 327
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKEL------------------EKLEELKKKLAELEKKLDELEEELAELLKElEELGFE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 328 SLEETNRTLtSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLltertlktqavNKLAEIMNR-KEPV 406
Cdd:PRK03918 586 SVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE-----------KRLEELRKElEELE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 407 KRGNDTDVRRKEKENRKLHME---LKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMtLDSKDSDIEQLRSQLQA 483
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKK 732
|
.
gi 194387796 484 L 484
Cdd:PRK03918 733 Y 733
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
51-288 |
4.37e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 51 QLKVIQQSLEQEEAEHKATKARladknkiyesiEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRcslldcdLKQSQ 130
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKE-----------EKALLKQLAALERRIAALARRIRALEQELAALEAE-------LAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 131 QKINELLKQKDVLNEDVRNLTLKIEQETQKRCLtqnDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKER 210
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPL---ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 211 QDADGQMKELQDQLEAEQyfstlykTQVRELKEECEEKTKLGKELQQKKQELQDERDSL---AAQLEITLTKADSEQLAR 287
Cdd:COG4942 167 AELEAERAELEALLAELE-------EERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAA 239
|
.
gi 194387796 288 S 288
Cdd:COG4942 240 A 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
25-482 |
6.55e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 25 LEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYE---SIEEAKSEAMKEMEKKLLEE 101
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITctaQCEKLEKIHLQESAQSLKER 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 102 RTLKQKVENLLLEAEKRCSL----------LDCDLKQSQQKINELLKQKDVLNEDVRNLtLKIEQETQKRCLTQNDLKMQ 171
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVvlarllelqeEPCPLCGSCIHPNPARQDIDNPGPLTRRM-QRGEQTYAQLETSEEDVYHQ 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 172 TQQV-NTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEEcEEKTK 250
Cdd:TIGR00618 551 LTSErKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-QDLQD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 251 LGKELQQKKQELQDERDSLaAQLEITLTKADSEQLARSIA--EEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIAS 328
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALSIRvlPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 329 LEETNRTLTSDVANLAN----EKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 404
Cdd:TIGR00618 709 LETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQ 788
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 405 PVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 482
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-464 |
7.87e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 10 EEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQ---SLEQEEAEHKATKARLADKNKIYESIEEA 86
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEissELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 87 KSEAMK-EMEKKLLEERtlkqkvenllleaekrcslldcdLKQSQQKINELLKQKDVLNEDVRNLTlKIEQETQKRcltq 165
Cdd:PRK03918 244 EKELESlEGSKRKLEEK-----------------------IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEY---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 ndlkmqtqqvntlkmseKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQleaeqyfstlyKTQVRELKEEC 245
Cdd:PRK03918 296 -----------------IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EEKTKLGKELQQKKQELQDERdSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKEL-EIKEMMARHKQELTEKDA 324
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIsKITARIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 325 TIASLEET-------NRTLTSDvaNLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAvNKLA 397
Cdd:PRK03918 427 AIEELKKAkgkcpvcGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAE 503
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194387796 398 EIMNRKEPVKRGNDTDVRRKEKENRKlhmeLKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQ 464
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
14-400 |
7.93e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 14 KNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKatkaRLADKNKIYESIEEAKSEAMKE 93
Cdd:COG5185 162 KDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNL----GSESTLLEKAKEIINIEEALKG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 94 MEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQkrcltQNDLKMQTQ 173
Cdd:COG5185 238 FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTK-----SIDIKKATE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 174 QVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQvRELKEECEEKTKLGK 253
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 254 ELQQKKQELQDERDSLAAQLEITLTKADS--EQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEE 331
Cdd:COG5185 392 SLDEIPQNQRGYAQEILATLEDTLKAADRqiEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDE 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387796 332 TNRTLTSdvanlanEKEELNNKLKDVQEQLSRLKDEEisaAAIKAQFEKQLLTERTLKTQAVNKLAEIM 400
Cdd:COG5185 472 INRSVRS-------KKEDLNEELTQIESRVSTLKATL---EKLRAKLERQLEGVRSKLDQVAESLKDFM 530
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
67-483 |
1.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 67 KATKARLADKNKIYESI----------EEAKSEAMK---EMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKI 133
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEErkaeearkaeDAKKAEAVKkaeEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 134 NELLKQKDVLN-EDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQD 212
Cdd:PTZ00121 1275 EEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 213 ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKlGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSI--A 290
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkA 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 291 EEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRtlTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIS 370
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 371 AAAIKAQFEKQLLTErtLKTQAVNKLAEIMNRKEPVKRGNDTdvrRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQ 450
Cdd:PTZ00121 1512 ADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADEL---KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
410 420 430
....*....|....*....|....*....|...
gi 194387796 451 AQIaEESQIRIELQMTLDSKDSDIEQLRSQLQA 483
Cdd:PTZ00121 1587 KKA-EEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
53-446 |
1.12e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 53 KVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLleaekRCSLLDCDLKQSQQK 132
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-----GSQDEESDLERLKEE 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 133 INELLKQKDVLNEDVRNLTLKIEQETQKR--CLTQNDLKMQTqqvntlkmsEKQLKQENNHLMEMKMNLEKQNAELRKER 210
Cdd:TIGR00606 648 IEKSSKQRAMLAGATAVYSQFITQLTDENqsCCPVCQRVFQT---------EAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 211 QDADGQMKELQDQLEAEQyfsTLYKTQVRELKEECEEKTKLGKELQQKKQELQdERDSLAAQLEITLTKADSEQLARSIA 290
Cdd:TIGR00606 719 KKKEKRRDEMLGLAPGRQ---SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIM 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 291 EEQYSDLEK-EKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEI 369
Cdd:TIGR00606 795 ERFQMELKDvERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 370 S---AAAIKAQFEKQLLTERT-------LKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLtQQM 439
Cdd:TIGR00606 875 QigtNLQRRQQFEEQLVELSTevqslirEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV-KNI 953
|
....*..
gi 194387796 440 IKYQKEL 446
Cdd:TIGR00606 954 HGYMKDI 960
|
|
| C1_nPKC_theta-like_rpt1 |
cd20834 |
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
616-673 |
1.27e-05 |
|
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410384 Cd Length: 61 Bit Score: 43.47 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMDKkeeIIAPC 673
Cdd:cd20834 5 VKGHEFIAKFFRQPTFCSVCKEFLWGFNK--QGYQCRQCNAAVHKKCHDK---ILGKC 57
|
|
| C1_RASGRP |
cd20808 |
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ... |
619-674 |
1.65e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410358 Cd Length: 52 Bit Score: 42.71 E-value: 1.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKDHmdkKEEIIAPCK 674
Cdd:cd20808 2 HNFQETTYFKPTFCDHCTGLLWGLIKQ--GYKCKDCGINCHKHC---KDLVVVECR 52
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-482 |
2.32e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 10 EEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSE 89
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 90 AMKEMEKKLLEERTLKQKVENLLLEAEKrcslLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLK 169
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKK----AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 170 --MQTQQVNTlKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEE 247
Cdd:pfam02463 374 elLAKKKLES-ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 248 KTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIA 327
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 328 SLEETNRTLtsDVANLANEKEELNNKLKDVQEQLSRLKDEE---ISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKE 404
Cdd:pfam02463 533 DLGVAVENY--KVAISTAVIVEVSATADEVEERQKLVRALTelpLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 405 PVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 482
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-490 |
2.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 318 ELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE------EISAAAIKAQFEKQLLTERTLKTQ 391
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidklqaEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 392 ----AVNKLAEIMNRKEP---VKRGndTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQ 464
Cdd:COG3883 97 rsggSVSYLDVLLGSESFsdfLDRL--SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180
....*....|....*....|....*.
gi 194387796 465 MTLDSKDSDIEQLRSQLQALHIGLDS 490
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE 200
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7-438 |
2.59e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 7 CGLEEDLKNgkillAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEA 86
Cdd:pfam05483 359 CSLEELLRT-----EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 87 KSEAMKEMEKKLleeRTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQK---DVLNEDVRNLTLKIEQETQKRCL 163
Cdd:pfam05483 434 LKGKEQELIFLL---QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASD 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 164 TQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMN----LEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVR 239
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 240 ELKEEC-------EEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLeKEKIMKELEIKEMM 312
Cdd:pfam05483 591 ILENKCnnlkkqiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-IDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 313 ARHKQELTEK-DATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEIsaAAIKAQFEKQLLTERTLKTQ 391
Cdd:pfam05483 670 EEKLLEEVEKaKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSEL--GLYKNKEQEQSSAKAALEIE 747
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 194387796 392 AVNKLAEIMNRKEPVkrgndtDVRRKEKEnrKLHMELKSEREKLTQQ 438
Cdd:pfam05483 748 LSNIKAELLSLKKQL------EIEKEEKE--KLKMEAKENTAILKDK 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
51-295 |
3.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 51 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQ 130
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 131 QK------INELLKQKDVlnEDVrnltlkIEQETQKRCLTQNDLKMQTQQvntlkmseKQLKQEnnhLMEMKMNLEKQNA 204
Cdd:COG3883 97 RSggsvsyLDVLLGSESF--SDF------LDRLSALSKIADADADLLEEL--------KADKAE---LEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 205 ELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQ 284
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|.
gi 194387796 285 LARSIAEEQYS 295
Cdd:COG3883 238 AAAAAAASAAG 248
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
191-485 |
3.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 191 HLMEMKMNLEkQNAELRKERQDAdgqmkelQDQLEAEQYfstLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLA 270
Cdd:PRK04863 277 HANERRVHLE-EALELRRELYTS-------RRQLAAEQY---RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 271 AQLEITLTKADSEQL---------ARSIAEEQYSDLEKEKIMKELEIKEM---MARHKQ--ELTEKDA-----TIASLEE 331
Cdd:PRK04863 346 QQEKIERYQADLEELeerleeqneVVEEADEQQEENEARAEAAEEEVDELksqLADYQQalDVQQTRAiqyqqAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 332 TNRTLTSD---VANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK----------------------QLLTE- 385
Cdd:PRK04863 426 AKQLCGLPdltADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarELLRRl 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 386 RTLKTQAV------NKLAEIMNRKEPVKRGNdtdvRRKEKENRKLHMELKSErEKLTQQMIKYQKELNEMQAQIAEESQI 459
Cdd:PRK04863 506 REQRHLAEqlqqlrMRLSELEQRLRQQQRAE----RLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|....*.
gi 194387796 460 RIELQMTLDSKDSDIEQLRSQLQALH 485
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWL 606
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
28-288 |
4.07e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 28 RQLQER----FTDLEKEKSNMEIdmtyqlkviqqsleqEEAEHKATKA-RLADKNKIYESIEEAKSEAMKEMEKKLLEEr 102
Cdd:PRK05771 23 EALHELgvvhIEDLKEELSNERL---------------RKLRSLLTKLsEALDKLRSYLPKLNPLREEKKKVSVKSLEE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 103 tLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLnEDVRNLTLKIEQETQKRCLTQ----------NDLKMQT 172
Cdd:PRK05771 87 -LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFKYVSVfvgtvpedklEELKLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 173 QQVNTLKMSEKqlKQENNHLMemkMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTlYKTQVRELKEEceeKTKLG 252
Cdd:PRK05771 165 DVENVEYISTD--KGYVYVVV---VVLKELSDEVEEELKKLGFERLELEEEGTPSELIRE-IKEELEEIEKE---RESLL 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 194387796 253 KELQQKKQELQDERDSLAAQLEITLTKAD-SEQLARS 288
Cdd:PRK05771 236 EELKELAKKYLEELLALYEYLEIELERAEaLSKFLKT 272
|
|
| C1_Myosin-IXa |
cd20883 |
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ... |
616-660 |
4.14e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410433 Cd Length: 58 Bit Score: 41.88 E-value: 4.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 660
Cdd:cd20883 3 HNGHIFKSTQYSIPTYCEYCSSLIWMMDR---AYVCKLCRYACHK 44
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-503 |
4.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 24 ELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKiyESIEEAKSEamKEMEKKLLEErt 103
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEAKKA--DEAKKKAEEA-- 1495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 104 lKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDvrnltlKIEQETQKRCLTQNDLKMQTQQVNTLKMSEK 183
Cdd:PTZ00121 1496 -KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD------EAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 184 QLKQENNHLMEMKMNLEKQNAElrKERQDADGQMKELQDQLEAEQYF-STLYKTQVRELKEECEEKTKLGkelQQKKQEL 262
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKkAEEAKIKAEELKKAEEEKKKVE---QLKKKEA 1643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 263 QDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVan 342
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-- 1721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 343 lanEKEELNNKLKdvQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRgndtDVRRKEKENR 422
Cdd:PTZ00121 1722 ---KKAEEENKIK--AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE----EELDEEDEKR 1792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 423 KLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRiELQMTLDSKDSDIEQLRSQLQAlhiGLDSSSIGSGPGDAEA 502
Cdd:PTZ00121 1793 RMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS-AIKEVADSKNMQLEEADAFEKH---KFNKNNENGEDGNKEA 1868
|
.
gi 194387796 503 D 503
Cdd:PTZ00121 1869 D 1869
|
|
| C1_RASSF1-like |
cd20820 |
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ... |
618-659 |
5.50e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410370 Cd Length: 52 Bit Score: 41.27 E-value: 5.50e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194387796 618 GHEFIPTLYHFPTNCEACMKPLWHMFkpPPALECRRCHIKCH 659
Cdd:cd20820 1 GHRFVPLELEQPTWCDLCGSVILGLF--RKCLRCANCKMTCH 40
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
199-385 |
5.56e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 199 LEKQNAELRKERQDADGQMKELQDQLEAEQyfstlyktqvrelkeecEEKTKLGKELQQKKQELQDERDSLaaqleitlt 278
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAK-----------------TELEDLEKEIKRLELEIEEVEARI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 279 KADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQ 358
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|....*..
gi 194387796 359 EQLSRLKDEeisAAAIKAQFEKQLLTE 385
Cdd:COG1579 156 AELEELEAE---REELAAKIPPELLAL 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-358 |
5.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 105 KQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNE---------DVRNLTLKIEQ-ETQKRCLTQN--DLK 169
Cdd:COG4913 609 RAKLAALeaeLAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAElEAELERLDASsdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 170 MQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDAD------GQMKELQDQLEAEQYFSTLYKTQVRElke 243
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQdrleaaEDLARLELRALLEERFAAALGDAVER--- 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 244 eceektKLGKELQQKKQELQDERDSLAAQLEITLT------KADSEQLARSIAE-EQYsdlekEKIMKELEiKEMMARHK 316
Cdd:COG4913 766 ------ELRENLEERIDALRARLNRAEEELERAMRafnrewPAETADLDADLESlPEY-----LALLDRLE-EDGLPEYE 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 194387796 317 QELTE--KDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQ 358
Cdd:COG4913 834 ERFKEllNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
10-209 |
6.56e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.19 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 10 EEDLKNGKilLAKVELEKR--QLQerftdLEKEKsnmeidmtyQLKVIQqSLEQEEAEHKATKARLADKnkiYESIEEAK 87
Cdd:pfam10168 546 EEYLKKHD--LAREEIQKRvkLLK-----LQKEQ---------QLQELQ-SLEEERKSLSERAEKLAEK---YEEIKDKQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 88 SEAMKEMEKKLleeRTLKQKVENLLlEAEKrcslldcDLKQSQQKINELLKQKDVlnedvRNLTLKIEQETQKRCLTQNd 167
Cdd:pfam10168 606 EKLMRRCKKVL---QRLNSQLPVLS-DAER-------EMKKELETINEQLKHLAN-----AIKQAKKKMNYQRYQIAKS- 668
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 194387796 168 lkMQTQQVNTLKMSEKQLKQENNHLMEMK---MNLEKQNAELRKE 209
Cdd:pfam10168 669 --QSIRKKSSLSLSEKQRKTIKEILKQLGseiDELIKQVKDINKH 711
|
|
| C1_SpBZZ1-like |
cd20824 |
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ... |
619-659 |
6.66e-05 |
|
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410374 Cd Length: 53 Bit Score: 41.15 E-value: 6.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCH 659
Cdd:cd20824 2 HNFKPHSFSIPTKCDYCGEKIWGLSK--KGLSCKDCGFNCH 40
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
511-593 |
7.18e-05 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 42.54 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 511 LEGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQCNPYMVLDIDKLFhVRPVTQTdvyraDAKEIPRIFQILY 590
Cdd:smart00233 3 KEGWLY--KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCT-VREAPDP-----DSSKKPHCFEIKT 74
|
...
gi 194387796 591 ANE 593
Cdd:smart00233 75 SDR 77
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-446 |
8.64e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 34 FTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERtlkQKVENLll 113
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR---DKANQL-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 114 eaEKRCSLLDCDLKQSQQKINELLKQ--------------KDVLNEDVRNLTLKIEQETQKR--------------CLTQ 165
Cdd:pfam05483 274 --EEKTKLQDENLKELIEKKDHLTKEledikmslqrsmstQKALEEDLQIATKTICQLTEEKeaqmeelnkakaahSFVV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 NDLKMQTQQVNTLKMSEKQ-LKQENNHLMEMKMNLEKQNAELRkerqdadgQMKELQDQLEAEQYFSTLYKTQVRELKEE 244
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELE--------EMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 245 CEEKTKLGKELQQKKQELQ---DERDSLAAQLEITLTK-ADSEQLARSIAEEQYSDLEKEKI----------MKELEIKE 310
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIfllQAREKEIHDLEIQLTAiKTSEEHYLKEVEDLKTELEKEKLknieltahcdKLLLENKE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 311 MMARHKQ---ELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE--------EISAAAIKAQFE 379
Cdd:pfam05483 504 LTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEvkckldksEENARSIEYEVL 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 380 KQLLTERTLKTQAVNKLAEIMNRK---EPVKRGNDTDVRRKEKENR----------KLHMELKSEREKLTQQMIKYQKEL 446
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNkniEELHQENKALKKKGSAENKqlnayeikvnKLELELASAKQKFEEIIDNYQKEI 663
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
55-482 |
8.98e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 55 IQQSLE------QEEAEHKATKARLADKNKIYESIEEAKSEaMKEMEKKLLE-ERTLKQKVENLL-----LEAEKRCSLL 122
Cdd:PRK11281 41 VQAQLDalnkqkLLEAEDKLVQQDLEQTLALLDKIDRQKEE-TEQLKQQLAQaPAKLRQAQAELEalkddNDEETRETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 123 DCDLKQSQQKINELLKQKDVLNEDVRNL-TLKIEQETQ----KRCLTQNdlKMQTQQVNTLKMSEKQLKQENNHLMEMKM 197
Cdd:PRK11281 120 TLSLRQLESRLAQTLDQLQNAQNDLAEYnSQLVSLQTQperaQAALYAN--SQRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 198 N-----LEKQNAELRKERQDADgqmkELQDqleaeqyfstLYKTQvRELKEECEEKtklgkeLQQKKQELQDE-RDSLAA 271
Cdd:PRK11281 198 QaeqalLNAQNDLQRKSLEGNT----QLQD----------LLQKQ-RDYLTARIQR------LEHQLQLLQEAiNSKRLT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 272 QLEITLTKADSEQLARSIaeeQYSDLekekIMKELEIkemmarhKQELTEKdaTIASLEETNrTLTSDvaNLANeKEELN 351
Cdd:PRK11281 257 LSEKTVQEAQSQDEAARI---QANPL----VAQELEI-------NLQLSQR--LLKATEKLN-TLTQQ--NLRV-KNWLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 352 NKLkdvqeQLSRLKDEEISA-------AAIKAQfEKQLLTERTLKTQAVNKLA-------EIMNRKEPVKRGND--TDVR 415
Cdd:PRK11281 317 RLT-----QSERNIKEQISVlkgslllSRILYQ-QQQALPSADLIEGLADRIAdlrleqfEINQQRDALFQPDAyiDKLE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387796 416 RKEKE--NRKLHMELKS---EREKLTQQMIkyqKELNemqAQIAEEsqirIELQMTLDSKDSDIEQLRSQLQ 482
Cdd:PRK11281 391 AGHKSevTDEVRDALLQlldERRELLDQLN---KQLN---NQLNLA----INLQLNQQQLLSVSDSLQSTLT 452
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
56-484 |
9.41e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 56 QQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKvenlLLEAEKRCSLLDCDLKQSQQKINE 135
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQ----LAHAKKQQELQQRYAELCAAAITC 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 136 LLKQKDVLNEDVRNLTLKIEQETQKrcltQNDLKMQTQQVNTLKMSEKQLKQEnnhLMEMKMNLEKQNAELRKERQDADg 215
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQ----LQTKEQIHLQETRKKAVVLARLLE---LQEEPCPLCGSCIHPNPARQDID- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 216 QMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQleITLTKADSEQLarsiaeEQYS 295
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC--DNRSKEDIPNL------QNIT 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 296 DLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNnklkdvQEQLSRLKDEEISAAAIK 375
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREHALSI 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 376 AQFEKQLLTERTLKTQA-------VNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNE 448
Cdd:TIGR00618 668 RVLPKELLASRQLALQKmqsekeqLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
410 420 430
....*....|....*....|....*....|....*.
gi 194387796 449 MQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
202-480 |
9.69e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 202 QNAELRKERQDADGQMKELQDQLEAeqyfstlyktQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKAD 281
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVE----------MARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 282 SEQL---------ARSIAEEQYSDLEKEKIMKELEIKEM---MARHKQELTEKDA-------TIASLEETNRTLTSD--- 339
Cdd:COG3096 356 LEELterleeqeeVVEEAAEQLAEAEARLEAAEEEVDSLksqLADYQQALDVQQTraiqyqqAVQALEKARALCGLPdlt 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 340 VANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK----------------------QLLTE-RTLKTQAVN-- 394
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageversqawqtarELLRRyRSQQALAQRlq 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 395 ----KLAEIMNRKEpvkrgNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSK 470
Cdd:COG3096 516 qlraQLAELEQRLR-----QQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
|
330
....*....|
gi 194387796 471 DSDIEQLRSQ 480
Cdd:COG3096 591 RARIKELAAR 600
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
51-365 |
9.75e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 51 QLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLleerTLKQKVENLLLEAEKRCSLLDCDLKQSQ 130
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI----RLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 131 QKINELLKQKDVLNEDVRNLTLKIEQETQ--KRCLTQNDLKMQTQQvntlkmSEKQLKQENNHLMEMKM-NLEKQNAELR 207
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSelRRQIQRAELELQSTN------SELEELQERLDLLKAKAsEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 208 ---KERQDADGQMKELQDQLEAEQYFSTLYKTqvreLKEECEEKTKLGKELQQKKQ------ELQDERDSLAAQLEITLT 278
Cdd:pfam05557 160 kqqSSLAEAEQRIKELEFEIQSQEQDSEIVKN----SKSELARIPELEKELERLREhnkhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 279 KADSEQLARsiAEEQYSDLEKEKIMKEL----------------------EIKEMMAR---HKQELTEKDATIASLEETN 333
Cdd:pfam05557 236 KLEREEKYR--EEAATLELEKEKLEQELqswvklaqdtglnlrspedlsrRIEQLQQReivLKEENSSLTSSARQLEKAR 313
|
330 340 350
....*....|....*....|....*....|..
gi 194387796 334 RTLTSDVANLANEKEELNNKLKDVQEQLSRLK 365
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9-452 |
1.02e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKS 88
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 EAMKEMEKKLLEERTLKQKVENLLLEAEkrcslldcDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNdL 168
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQS--------SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-I 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 169 KMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEK 248
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 249 TKLGKELQQKKQELQDERdslaaqlEITLTKADSEQLARSIAEEQYsdlEKEKIMKELEIKEMMARHKQELTEKDAT-IA 327
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKE-------QIHLQETRKKAVVLARLLELQ---EEPCPLCGSCIHPNPARQDIDNPGPLTRrMQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 328 SLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEeisaaaikaqfEKQLLTERTLKTQAVNKLAEIMNRKEPVK 407
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-----------FSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 194387796 408 RGNDtdvrrkeKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQ 452
Cdd:TIGR00618 601 EKLS-------EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
225-464 |
1.25e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 225 EAEQYFSTLYK---TQVRELKEE-----CEEKTKLGKELQQKKQELQDERD--SLAAQLEITLTKADSEQLARSIAEEqY 294
Cdd:PRK05771 17 YKDEVLEALHElgvVHIEDLKEElsnerLRKLRSLLTKLSEALDKLRSYLPklNPLREEKKKVSVKSLEELIKDVEEE-L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 295 SDLEKE--KIMKEL-EIKEMMARHKQELTE----KDATIA-SLEETNRTLTSDVANLANEKEELNNKLKD--VQEQLSRL 364
Cdd:PRK05771 96 EKIEKEikELEEEIsELENEIKELEQEIERlepwGNFDLDlSLLLGFKYVSVFVGTVPEDKLEELKLESDveNVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 365 KDEEISAAAIKAQFEKQLLTErtlktqavnkLAEIMNRKEPVKRGNDTDVRRKEKENRKlhMELKSEREKLTQQMIKYQK 444
Cdd:PRK05771 176 KGYVYVVVVVLKELSDEVEEE----------LKKLGFERLELEEEGTPSELIREIKEEL--EEIEKERESLLEELKELAK 243
|
250 260
....*....|....*....|
gi 194387796 445 ELNEMQAQIAEESQIRIELQ 464
Cdd:PRK05771 244 KYLEELLALYEYLEIELERA 263
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-462 |
2.31e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQErftDLEKEKSNME--IDMT-----------YQLKVIQQSLEQEEAEHKATKARLAD 75
Cdd:pfam01576 276 LQEDLESERAARNKAEKQRRDLGE---ELEALKTELEdtLDTTaaqqelrskreQEVTELKKALEEETRSHEAQLQEMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 76 K-----NKIYESIEEAK-SEAMKEMEKKLLEERTLKQKVENLLL-----EAEKRCSLLDCDLKQSQQKINELLKQKDVLN 144
Cdd:pfam01576 353 KhtqalEELTEQLEQAKrNKANLEKAKQALESENAELQAELRTLqqakqDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 145 EDVRNLTLKIE------QETQKRCL---------------TQNDLKMQTQQVNTLKMSEKQLKQENNHLMEM-------K 196
Cdd:pfam01576 433 EKLSKLQSELEsvssllNEAEGKNIklskdvsslesqlqdTQELLQEETRQKLNLSTRLRQLEDERNSLQEQleeeeeaK 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 197 MNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLE-- 274
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDhq 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 275 ---ITLTKADSEQLARSIAEE-----QYSDlEKEKIMKELEIKEM----MARHKQELTEkdaTIASLEETNRTLTSDVAN 342
Cdd:pfam01576 593 rqlVSNLEKKQKKFDQMLAEEkaisaRYAE-ERDRAEAEAREKETralsLARALEEALE---AKEELERTNKQLRAEMED 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 343 LANEKEE--------------LNNKLKDVQEQLSRLKDE-----------EISAAAIKAQFEKqlltertlktqavnkla 397
Cdd:pfam01576 669 LVSSKDDvgknvhelerskraLEQQVEEMKTQLEELEDElqatedaklrlEVNMQALKAQFER----------------- 731
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 398 EIMNRKEPvkrgNDTDVRRKEKENRKLHMELKSEREKLTQQMI---KYQKELNEMQAQIAEESQIRIE 462
Cdd:pfam01576 732 DLQARDEQ----GEEKRRQLVKQVRELEAELEDERKQRAQAVAakkKLELDLKELEAQIDAANKGREE 795
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
52-482 |
2.45e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 52 LKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEME--KKLLEErtlkqkvENLLLEAEKRCSLLDCDLKQS 129
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelKKILAE-------DEKLLDEKKQFEKIAEELKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 130 QQKINELLKQKDvlnEDVRNLTLKIEqetqkrcLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKE 209
Cdd:pfam05483 438 EQELIFLLQARE---KEIHDLEIQLT-------AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 210 RQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEEceeKTKLGKELQQKKQELQDERDSLAAQLEitltkaDSEQLARSI 289
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK---EMNLRDELESVREEFIQKGDEVKCKLD------KSEENARSI 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 290 aeeQYSDLEKEKIMKELEIKemMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKD--E 367
Cdd:pfam05483 579 ---EYEVLKKEKQMKILENK--CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQkfE 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 368 EISAAAIKAQFEKQLLTERTLktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMikyQKELN 447
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLL--EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELG 728
|
410 420 430
....*....|....*....|....*....|....*
gi 194387796 448 EMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 482
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLE 763
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
25-484 |
2.74e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 25 LEKRQLQERFTDLekeKSNMEidmtyQLKVIQQSLEQEEAEHKAtkarLADKNKIYESIEEAKSEAMkemEKKLLEERTL 104
Cdd:COG4913 218 LEEPDTFEAADAL---VEHFD-----DLERAHEALEDAREQIEL----LEPIRELAERYAAARERLA---ELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 105 KQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRcLTQ--NDLKMQTQQVNTLKMSE 182
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR-LEQleREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 183 KQLKQENNHLmEMKMNLEKQN-AELRKERQDADGQMKELQDQLEAEQYFStlyKTQVRELKEECEEKTKLGKELQQKK-- 259
Cdd:COG4913 362 ARLEALLAAL-GLPLPASAEEfAALRAEAAALLEALEEELEALEEALAEA---EAALRDLRRELRELEAEIASLERRKsn 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 260 --QELQDERDSLAAQLEITLT-----------KADSEQ-----------LARSI--AEEQYSDLEK-------------E 300
Cdd:COG4913 438 ipARLLALRDALAEALGLDEAelpfvgelievRPEEERwrgaiervlggFALTLlvPPEHYAAALRwvnrlhlrgrlvyE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 301 KIMKELEIKEMMARHKQELTEK--------------------D----ATIASLEETNRTLTSD----------------- 339
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAGKldfkphpfrawleaelgrrfDyvcvDSPEELRRHPRAITRAgqvkgngtrhekddrrr 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 340 --------------VANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEK-QLLTERTLKT-QAVNKLAEIMNRK 403
Cdd:COG4913 598 irsryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVaSAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 404 EPVKRGNDtDVRrkekenrklhmELKSEREKLtqqmikyQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQA 483
Cdd:COG4913 678 ERLDASSD-DLA-----------ALEEQLEEL-------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
.
gi 194387796 484 L 484
Cdd:COG4913 739 A 739
|
|
| C1_RASSF1 |
cd20885 |
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ... |
616-659 |
3.11e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410435 Cd Length: 54 Bit Score: 39.17 E-value: 3.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCH 659
Cdd:cd20885 1 GEGHDFQPCSLTNPTWCDLCGDFIWGLYKQ--CLRCTHCKYTCH 42
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
104-289 |
3.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 104 LKQKVENLLLEAEKRCSLLdcdLKQSQQKINELLKQKDV-LNEDVRNLTLKIEQETQKRcltQNDLKMQtqqvntlkmsE 182
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRI---LEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRER---RNELQKL----------E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 183 KQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELqDQLEAEqyfstlYKTQVRELKEECEEKTKLGKE------LQ 256
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL-EKKEEE------LEELIEEQLQELERISGLTAEeakeilLE 161
|
170 180 190
....*....|....*....|....*....|...
gi 194387796 257 QKKQELQDERDSLAAQLEiTLTKADSEQLARSI 289
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIE-EEAKEEADKKAKEI 193
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
77-479 |
3.56e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 77 NKIYESIEEAKsEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCdlkqsQQKINELLKQKDVlNEDVRNLTLKIEQ 156
Cdd:TIGR01612 1358 NKIKKIIDEVK-EYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEEC-----KSKIESTLDDKDI-DECIKKIKELKNH 1430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 157 ETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMkMNLEKQNAElrkerQDADGQMKELQDQLEAeqyfSTLYKT 236
Cdd:TIGR01612 1431 ILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHI-LKIKKDNAT-----NDHDFNINELKEHIDK----SKGCKD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 237 QVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIaeeqySDLEKEKIMKELEIKEMMARHK 316
Cdd:TIGR01612 1501 EADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEI-----KDAHKKFILEAEKSEQKIKEIK 1575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 317 QELTEKDATIASLEETNRT---LTSDVANLANEKEELNNKLKDVQEQLSRLK--DEEISAAAIKAQfekqlLTERTLKTQ 391
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAaidIQLSLENFENKFLKISDIKKKINDCLKETEsiEKKISSFSIDSQ-----DTELKENGD 1650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 392 AVNKLAEIMNRKEPVKRgndtDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIElqMTLDSKD 471
Cdd:TIGR01612 1651 NLNSLQEFLESLKDQKK----NIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIE--SIKELIE 1724
|
....*...
gi 194387796 472 SDIEQLRS 479
Cdd:TIGR01612 1725 PTIENLIS 1732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
38-404 |
3.91e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 38 EKEKSNMEIDmtyQLKVIQQSLEQE-EAEHKATKARLADKNKIYESIEE--AKSEAMKEMEKKLLEERTLKQKVenlLLE 114
Cdd:pfam15921 420 ELDDRNMEVQ---RLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEELTAKKMT---LES 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 115 AEKRCSLLDCDLKQSQQKIN----ELLKQKDVLNEDVRNLT-LKIEQETQKRCLTQND-LKMQT-----------QQVNT 177
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECEaLKLQMaekdkvieilrQQIEN 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 178 L--------------KMSEKQLKQENN----HLMEMKMNLEKQNAELRK--------------------ERQDADGQMKE 219
Cdd:pfam15921 574 MtqlvgqhgrtagamQVEKAQLEKEINdrrlELQEFKILKDKKDAKIRElearvsdlelekvklvnagsERLRAVKDIKQ 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 220 LQDQLEAEqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITltKADSEQLARSIAEEQYSDLEK 299
Cdd:pfam15921 654 ERDQLLNE------VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA--QSELEQTRNTLKSMEGSDGHA 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 300 EKIMKELEiKEMMARHKQ--------ELTEKDATIAS-----LEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKD 366
Cdd:pfam15921 726 MKVAMGMQ-KQITAKRGQidalqskiQFLEEAMTNANkekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 194387796 367 E----EISAAAIKAQF-EKQLLTERTLKTQAVNKLAEIMNRKE 404
Cdd:pfam15921 805 KvanmEVALDKASLQFaECQDIIQRQEQESVRLKLQHTLDVKE 847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
126-485 |
4.24e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 126 LKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEK--QN 203
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 204 AELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAA----QLEITLTK 279
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 280 ADSEQLARSIAEEQYSDLEKE-----KIMKELEIKEMMARHKQELTEKD------ATIASLEETNRTLTSDVANLA---- 344
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEEleeleEELEQLENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAgvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 345 --------------NEKEELNNKLKDVQ--EQLSRLKDEEISAAAIKAQFEKQLLTERTLK-----TQAVNKLAEIMNRK 403
Cdd:COG4717 281 lvlgllallflllaREKASLGKEAEELQalPALEELEEEELEELLAALGLPPDLSPEELLElldriEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 404 EPVKR----------------GNDTDVRRKEKENRKLHmELKSEREKLTQQMIKYQKELNEMQAQIAEES-QIRI-ELQM 465
Cdd:COG4717 361 EELQLeeleqeiaallaeagvEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEElEEELeELEE 439
|
410 420
....*....|....*....|
gi 194387796 466 TLDSKDSDIEQLRSQLQALH 485
Cdd:COG4717 440 ELEELEEELEELREELAELE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
24-455 |
4.81e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 24 ELEKRQLQERFTDLEKEksnmeidmtyqLKVIQQSLEQEEAEHKATKARLADknkIYESIEEAKSEAMKEMEKKLLEERT 103
Cdd:COG4913 287 QRRLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDE---LEAQIRGNGGDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 104 LKQKVENLLLEAEKRCSLLDCDLKQSQqkinellkqkDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEK 183
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 184 QLKQENNHLMEMKMNLEKQNAELRKERQDADG-------------QMKELQD--QLEAEQYFSTL---------YKTQVR 239
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALGldeaelpfvgeliEVRPEEErwRGAIERVLGGFaltllvppeHYAAAL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 240 ELKEEceekTKLGKELQ--------QKKQELQDERDSLAAQLEITLTKADS---EQLARSIA------EEQYSDLEKeKI 302
Cdd:COG4913 503 RWVNR----LHLRGRLVyervrtglPDPERPRLDPDSLAGKLDFKPHPFRAwleAELGRRFDyvcvdsPEELRRHPR-AI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 303 MKELEIKEMMARHkqeltEKDATIASLEE-----TNR----TLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAA 373
Cdd:COG4913 578 TRAGQVKGNGTRH-----EKDDRRRIRSRyvlgfDNRaklaALEAELAELEEELAEAEERLEALEAELDALQERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 374 IKAQFEKQLLTErtlktQAVNKLAEIMNRKEPVKRGNDT--DVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQA 451
Cdd:COG4913 653 LAEYSWDEIDVA-----SAEREIAELEAELERLDASSDDlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
....
gi 194387796 452 QIAE 455
Cdd:COG4913 728 ELDE 731
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
234-481 |
5.00e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 234 YKTQVRELKEECEEKTKLGK-----------ELQQKKQELQDERDSLAaqlEITLTKADSEQLARSIAEEQYSDLEKEKI 302
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEkqkfylrqsviDLQTKLQEMQMERDAMA---DIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 303 MKE----------LEIKEMMARHKQELTEKDATIASLEETN---------------RTLTSDVANLANEKEE----LNNK 353
Cdd:pfam15921 160 LKEdmledsntqiEQLRKMMLSHEGVLQEIRSILVDFEEASgkkiyehdsmstmhfRSLGSAISKILRELDTeisyLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 354 LKDVQEQLSRLKDEeisaaaikAQFEKQLLTErtlktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSERE 433
Cdd:pfam15921 240 IFPVEDQLEALKSE--------SQNKIELLLQ-----QHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 194387796 434 KLTQQMIKYQKELNEMQAQIaeeSQIRIELQMTLDSKDSDIEQLRSQL 481
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---SQLRSELREAKRMYEDKIEELEKQL 351
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
192-279 |
5.74e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 192 LMEMKMNLEKQNAELRKERQDADGQMKELQDQLEA-EQYFSTLYKTQ-------VRELKEECEEKTKLGKELQ------Q 257
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAekeaqqaIKEAKKEADEIIKELRQLQkggyasV 604
|
90 100
....*....|....*....|..
gi 194387796 258 KKQELQDERDSLAAQLEITLTK 279
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKK 626
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
99-484 |
7.40e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 99 LEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKmqtQQVNTL 178
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE---SRVAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 179 KMSEKQLKQENNHLMEMKMNLEKQNAELRKER-------QDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKL 251
Cdd:pfam07888 86 KEELRQSREKHEELEEKYKELSASSEELSEEKdallaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 252 GKELQQKKQELQDERDslAAQLEITLTKADSEQLARSIAeeqysdlekEKIMKELEIKEMMARHKQELTEKDATIASLEE 331
Cdd:pfam07888 166 RKEEEAERKQLQAKLQ--QTEEELRSLSKEFQELRNSLA---------QRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 332 TNRTLTSdvanlanekeeLNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEiMNRKEPVKRGNd 411
Cdd:pfam07888 235 LLEELRS-----------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAD-ASLALREGRAR- 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387796 412 tdvRRKEKENRKLHMELKSER-EKLTQQMIKYQKELnemQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQAL 484
Cdd:pfam07888 302 ---WAQERETLQQSAEADKDRiEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQEL 369
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
17-322 |
7.51e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 17 KILLAKVELEKRQLQERFTDLEKEKsnMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIY---ESIEEAKSEAMKE 93
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKI--DEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKtekLKVEEEKEEKLKA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 94 MEKKLLEERTLKQKVENLLLEAEKRCSLLDC----DLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLK 169
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKikeeELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 170 MQTQQVNTLKMSEKQLKQENNHLMEmkmNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKT 249
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELE---EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK 955
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387796 250 klgKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEK 322
Cdd:pfam02463 956 ---EEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9-483 |
7.97e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIdmtyQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKS 88
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSI----EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 E-AMKEMEKKLLEERTlkqkvenllleaEKRCSLLDCDLKQSQQKINELLKQKDVLnEDVRNLTLKIEQETQKRCLTQND 167
Cdd:PRK01156 264 DlSMELEKNNYYKELE------------ERHMKIINDPVYKNRNYINDYFKYKNDI-ENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 168 LKMQTQQVNTLKMSEKQLKQENNHLMEMK----------MNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQ 237
Cdd:PRK01156 331 LSVLQKDYNDYIKKKSRYDDLNNQILELEgyemdynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 238 VRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEI------------TLTKADSEQLARSIAEEQySDLEKEKIMKE 305
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvcgtTLGEEKSNHIINHYNEKK-SRLEEKIREIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 306 LEIKEMMARHKQELTEKDaTIASlEETNRTLTSDvanlaNEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFE------ 379
Cdd:PRK01156 490 IEVKDIDEKIVDLKKRKE-YLES-EEINKSINEY-----NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKslkled 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 380 --------------KQLLTERTLKTQ----------AVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMElKSEREKL 435
Cdd:PRK01156 563 ldskrtswlnalavISLIDIETNRSRsneikkqlndLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK-YNEIQEN 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 194387796 436 TQQMIKYQKELNEMQAQIAEESQIrIELQMTLDSKDSDIE----QLRSQLQA 483
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSI-IPDLKEITSRINDIEdnlkKSRKALDD 692
|
|
| C1_cPKC_nPKC_rpt1 |
cd20792 |
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ... |
618-660 |
8.27e-04 |
|
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410342 Cd Length: 53 Bit Score: 37.99 E-value: 8.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 194387796 618 GHEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 660
Cdd:cd20792 1 GHKFVATFFKQPTFCSHCKDFIWGLGKQ--GYQCQVCRFVVHK 41
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
114-482 |
8.27e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 114 EAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLM 193
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 194 EMKMNLEKQNAELRKERQDADGQMKelqdqleaeqyfstLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQL 273
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNID--------------KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 274 EITLTKADSEQLARSIAEEQYSDLEKekimkeleikemmarHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 353
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKK---------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 354 LKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKrgndtdvrrKEKENrKLHMELKSERE 433
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---------NQKEQ-DWNKELKSELK 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 194387796 434 KLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQ 482
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
|
| C1_dGM13116p-like |
cd20831 |
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ... |
616-660 |
9.12e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410381 Cd Length: 58 Bit Score: 38.09 E-value: 9.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 194387796 616 HKGHEFIPTlyHF--PTNCEACMKPLWHMF-KPppALECRRCHIKCHK 660
Cdd:cd20831 3 YNDHTFVAT--HFkgGPSCAVCNKLIPGRFgKQ--GYQCRDCGLICHK 46
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
280-401 |
9.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 280 ADSEQLARSIAEEQYSDLEKEKIMKELEIKEMM----ARHKQELTEKDATIASLEETnrtltsdvanLANEKEELNNKLK 355
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIhklrNEFEKELRERRNELQKLEKR----------LLQKEENLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 194387796 356 DVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMN 401
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG 149
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
52-289 |
9.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 52 LKVIQQSLEQEEAEHKATKARLAD---KNKIYESIEEAKS--EAMKEMEKKLLEERTLKQKVENLLLEAEKRcslldcdL 126
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEfrqKNGLVDLSEEAKLllQQLSELESQLAEARAELAEAEARLAALRAQ-------L 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 127 KQSQQKINELLKQKDV--LNEDVRNLTLKIEQETQKrcLTQNDLKMQT--QQVNTLkmsEKQLKQEnnhlmemkmnLEKQ 202
Cdd:COG3206 250 GSGPDALPELLQSPVIqqLRAQLAELEAELAELSAR--YTPNHPDVIAlrAQIAAL---RAQLQQE----------AQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 203 NAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEeceektklgkeLQQKKQELQDERDSLAAQLEITLTKADS 282
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQ-------LEARLAELPE-----------LEAELRRLEREVEVARELYESLLQRLEE 376
|
....*..
gi 194387796 283 EQLARSI 289
Cdd:COG3206 377 ARLAEAL 383
|
|
| C1_MTMR-like |
cd20828 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ... |
619-659 |
9.99e-04 |
|
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410378 Cd Length: 57 Bit Score: 37.81 E-value: 9.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCH 659
Cdd:cd20828 6 HNFEPHSFVTPTNCDYCLQILWGIVK--KGMKCSECGYNCH 44
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
265-433 |
1.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 265 ERDSLAAQLEITLTKADS-EQLARSIAEeqYSDLEKEKI--------------MKELEIKEMMARHKQELTEKDATIASL 329
Cdd:COG2433 334 ERDALAAALKAYDAYKNKfERVEKKVPP--DVDRDEVKArvirglsieealeeLIEKELPEEEPEAEREKEHEERELTEE 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 330 EETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEeisaaaikAQFEKQLLTERTLKTQAVNKLAEIMNRKEpvkrg 409
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE--------LSEARSEERREIRKDREISRLDREIERLE----- 478
|
170 180
....*....|....*....|....
gi 194387796 410 ndTDVRRKEKENRKLHMELKSERE 433
Cdd:COG2433 479 --RELEEERERIEELKRKLERLKE 500
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
296-486 |
1.09e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 296 DLEKEKI-MKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAI 374
Cdd:PHA02562 191 DHIQQQIkTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 375 KAQFEK--QLLTERTL---KTQAVNKLAEIMnrkepvkrgndTDVRRKEKENRKLHMELKSEREKLTQQMIKY---QKEL 446
Cdd:PHA02562 271 IEQFQKviKMYEKGGVcptCTQQISEGPDRI-----------TKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqSKKL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 194387796 447 NEMQAQIAEESQIRIelqmTLDSKDSDIEQLRSQLQALHI 486
Cdd:PHA02562 340 LELKNKISTNKQSLI----TLVDKAKKVKAAIEELQAEFV 375
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
233-398 |
1.34e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.35 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 233 LYKTQVRELKEECE----EKTKLGKELQQKKQELQderdSLAAQLEitltkaDSEQLARSIaEEQYSDLEKEKIMKELEI 308
Cdd:pfam05911 678 LKTEENKRLKEEFEqlksEKENLEVELASCTENLE----STKSQLQ------ESEQLIAEL-RSELASLKESNSLAETQL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 309 KEMMARHKQ---ELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIkAQFEKQLLTE 385
Cdd:pfam05911 747 KCMAESYEDletRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDA-DQEDKKLQQE 825
|
170
....*....|...
gi 194387796 386 RTLkTQAVNKLAE 398
Cdd:pfam05911 826 KEI-TAASEKLAE 837
|
|
| C1_ARHGEF-like |
cd20832 |
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ... |
618-668 |
1.38e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410382 Cd Length: 53 Bit Score: 37.35 E-value: 1.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 194387796 618 GHEFIPTLYHFPTNCEACMKPLWHMfkPPPALECRRCHIKCHKDHMDKKEE 668
Cdd:cd20832 1 GHQFVLQHYYQVTFCNHCSGLLWGI--GYQGYQCSDCEFNIHKQCIEVIEE 49
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
207-477 |
1.47e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 207 RKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKL--GKELQQKKQELQDERDSLAAQLEITLTKADSEQ 284
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLrtVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 285 LARSIAEEQYSDLEKEKIMKELEIKEmmarhKQELTEKDATIASLEETNRTLTsdvanlanEKEELNNKLKDVQEQLSRl 364
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAE-----KNILLLNQARLQALEDLEKILT--------EKEALQGKINILEMRLSE- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 365 KDEEISAAAiKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEkenrklHMELKSEREKLTQQMIKYQK 444
Cdd:PLN02939 182 TDARIKLAA-QEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE------NMLLKDDIQFLKAELIEVAE 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 194387796 445 ELNEMQAQIAE----ESQIRiELQMTLDSKDSDIEQL 477
Cdd:PLN02939 255 TEERVFKLEKErsllDASLR-ELESKFIVAQEDVSKL 290
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
17-381 |
1.53e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 17 KILLAKVELEKRQLQERFTDLE---KEKSNMEI--DMTYQLKVIQQSLEQEEAEHKATKARLADKNK--------IYESI 83
Cdd:COG5022 773 KIQVIQHGFRLRRLVDYELKWRlfiKLQPLLSLlgSRKEYRSYLACIIKLQKTIKREKKLRETEEVEfslkaevlIQKFG 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 84 EEAKSEAMKEMEKKLLEERTLKQKVENllleAEKRCSLLDCDLK-------QSQQKINELLKQKDVLNEDVR-NLTLKIE 155
Cdd:COG5022 853 RSLKAKKRFSLLKKETIYLQSAQRVEL----AERQLQELKIDVKsisslklVNLELESEIIELKKSLSSDLIeNLEFKTE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 156 QETQKRCLTQN-------DLKMQTQ-QVNTLKMSEKQLKQENnhlmEMKMNLEKQNAELRKERQDADGQMKELQDQLeae 227
Cdd:COG5022 929 LIARLKKLLNNidleegpSIEYVKLpELNKLHEVESKLKETS----EEYEDLLKKSTILVREGNKANSELKNFKKEL--- 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 228 qyfstlykTQVRELKEECEEKTKLGKELQQKKQELQderdslaaqleiTLTKADSEQlarSIAEEQYSDLEKEKIMKELE 307
Cdd:COG5022 1002 --------AELSKQYGALQESTKQLKELPVEVAELQ------------SASKIISSE---STELSILKPLQKLKGLLLLE 1058
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194387796 308 IKEMMARHKQELTEKDATIasLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQ 381
Cdd:COG5022 1059 NNQLQARYKALKLRRENSL--LDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
164-467 |
1.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 164 TQNDLKMQTQQVNTLKMSE------KQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstLYKTQ 237
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEaedklvQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA------LKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 238 VRELKEECE--EKTKLGKELQQKKQELQDERDSLA---AQLeITL-TKADSEQLARSIAEEQYSDLEKEKIMKELEIKEM 311
Cdd:PRK11281 111 DEETRETLStlSLRQLESRLAQTLDQLQNAQNDLAeynSQL-VSLqTQPERAQAALYANSQRLQQIRNLLKGGKVGGKAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 312 MARHKQELTEKDATIASLEETNRTLtsdvanLANekeelNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLkTQ 391
Cdd:PRK11281 190 RPSQRVLLQAEQALLNAQNDLQRKS------LEG-----NTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRL-TL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 392 AVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREK---LTQQMIKYQKEL-NEMQAQIAEESQIRIeLQMTL 467
Cdd:PRK11281 258 SEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKlntLTQQNLRVKNWLdRLTQSERNIKEQISV-LKGSL 336
|
|
| C1_nPKC_theta-like_rpt2 |
cd20837 |
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ... |
619-660 |
1.70e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410387 Cd Length: 50 Bit Score: 37.03 E-value: 1.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 660
Cdd:cd20837 1 HRFKVYNYMSPTFCDHCGSLLWGLFRQ--GLKCEECGMNVHH 40
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-366 |
1.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDmtyqLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKS 88
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD----LGNAEDFLEELREERDELREREAELEATLRTARERVE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 89 EAmkemeKKLLEE---RTLKQKVEnlllEAEKRCSLLDCDlkqsqQKINELLKQKDVLNEDVRNLTLKIEQETqkrcltq 165
Cdd:PRK02224 444 EA-----EALLEAgkcPECGQPVE----GSPHVETIEEDR-----ERVEELEAELEDLEEEVEEVEERLERAE------- 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 166 nDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQleaeqyfstlyktqVRELKEEC 245
Cdd:PRK02224 503 -DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA--------------AAEAEEEA 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEE-----QYSDLEKEKI------MKELE------- 307
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKrealaELNDERRERLaekrerKRELEaefdear 647
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194387796 308 ---IKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNN---KLKDVQEQLSRLKD 366
Cdd:PRK02224 648 ieeAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEElreRREALENRVEALEA 712
|
|
| C1_PKD2_rpt2 |
cd20843 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ... |
619-660 |
1.96e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410393 Cd Length: 79 Bit Score: 37.65 E-value: 1.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHK 660
Cdd:cd20843 12 HTFVIHSYTRPTVCQFCKKLLKGLFRQ--GLQCKDCKFNCHK 51
|
|
| C1_RASGRP1 |
cd20860 |
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ... |
619-674 |
2.40e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410410 Cd Length: 55 Bit Score: 36.83 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKPppALECRRCHIKCHKDHmdkKEEIIAPCK 674
Cdd:cd20860 3 HNFQETTYLKPTFCDNCAGFLWGVIKQ--GYRCKDCGMNCHKQC---KDLVVFECK 53
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9-456 |
2.49e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 9 LEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDM-----TYQLKVIQQSLEQEEAEHKATKARLADKNKIYESI 83
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQF 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 84 ---------------------EEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDV 142
Cdd:TIGR00606 669 itqltdenqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 143 LNEDVRNLTLKIEQEtqkrcltQNDLKMQTQQVNTLKMSEKQLK--QENNHLMEmKMNLEKQNAELRKERQDADGQMKEL 220
Cdd:TIGR00606 749 LRNKLQKVNRDIQRL-------KNDIEEQETLLGTIMPEEESAKvcLTDVTIME-RFQMELKDVERKIAQQAAKLQGSDL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 221 QdqleaeqyfstLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKE 300
Cdd:TIGR00606 821 D-----------RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 301 KIMKELEIKEMMarhkQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKD-VQEQLSRLKDEEISAAAIKAQFE 379
Cdd:TIGR00606 890 LVELSTEVQSLI----REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDkVNDIKEKVKNIHGYMKDIENKIQ 965
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194387796 380 KQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQ-KELNEMQAQIAEE 456
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENElKEVEEELKQHLKE 1043
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
511-593 |
2.73e-03 |
|
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 37.52 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 511 LEGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQcNPYMVLDIDKLFHVRPVTQtdvyradaKEIPRIFQILY 590
Cdd:cd00821 1 KEGYLL--KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSY-KPKGSIPLSGILEVEEVSP--------KERPHCFELVT 69
|
...
gi 194387796 591 ANE 593
Cdd:cd00821 70 PDG 72
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
76-359 |
2.84e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 76 KNKIYESIEEAKSEAMKEME-KKLLEERTlkqkvenlllEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKI 154
Cdd:pfam15905 62 KKKSQKNLKESKDQKELEKEiRALVQERG----------EQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 155 EQETQKRCLTQNDLKMQTQQvntlkmseKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLY 234
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQ--------KKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 235 KTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAA-QLEITLTKADSEQLARSIAEEQySDLEKEKIMKELEIKEMMA 313
Cdd:pfam15905 204 EEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKyKLDIAQLEELLKEKNDEIESLK-QSLEEKEQELSKQIKDLNE 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 194387796 314 RHKQELTEKDATIASLEETNRTLTSDVANLaneKEELNNKLKDVQE 359
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEEL---KEKLTLEEQEHQK 325
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-480 |
3.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 199 LEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLE---- 274
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEE-------LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecrv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 275 -ITLTKADSEQLARSIAEEQYSDLEKEKIMKELEikEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNK 353
Cdd:PRK02224 336 aAQAHNEEAESLREDADDLEERAEELREEAAELE--SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 354 LKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLktQAVNKLAEIMNRKEPVKRGNDTDVRRKEKEnrklhmELKSERE 433
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVEGSPHVETIEEDRERVE------ELEAELE 485
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 194387796 434 KLTQQMIKYQKELNEMQAQIAEESQIRielqmTLDSKDSDIEQLRSQ 480
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIE-----RLEERREDLEELIAE 527
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
95-300 |
3.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 95 EKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLK----- 169
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 170 MQTQ---------------------QVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEaeq 228
Cdd:COG3883 95 LYRSggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA--- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387796 229 yfstlyktqvrELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKE 300
Cdd:COG3883 172 -----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| C1_KSR |
cd20812 |
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ... |
619-665 |
3.38e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410362 Cd Length: 48 Bit Score: 36.15 E-value: 3.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 194387796 619 HEFIPTLYhFPTNCEACMKPLWHMFKpppaleCRRCHIKCHKDHMDK 665
Cdd:cd20812 3 HRFSKKLF-MRQTCDYCHKQMFFGLK------CKDCKYKCHKKCAKK 42
|
|
| C1_Raf |
cd20811 |
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ... |
619-660 |
3.43e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410361 Cd Length: 49 Bit Score: 36.12 E-value: 3.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKpppaleCRRCHIKCHK 660
Cdd:cd20811 3 HNFVRKTFFTLAFCDVCRKLLFQGFR------CQTCGFKFHQ 38
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
20-219 |
3.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 20 LAKVELEKRQLQERF-TDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARladknkiYESIEEAKSEAMKEMEKKL 98
Cdd:pfam17380 380 LERLQMERQQKNERVrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR-------QREVRRLEEERAREMERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 99 LEERTLKQKVENLLL-EAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNT 177
Cdd:pfam17380 453 LEEQERQQQVERLRQqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 194387796 178 LKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKE 219
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
512-597 |
3.82e-03 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 37.54 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 512 EGWLSlpVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQCNPYMVLDIDKlfhvrpVTQTDVYRADAKEIPRIFQILYA 591
Cdd:pfam00169 4 EGWLL--KKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSG------CEVVEVVASDSPKRKFCFELRTG 75
|
....*.
gi 194387796 592 NEGESK 597
Cdd:pfam00169 76 ERTGKR 81
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
173-435 |
3.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 173 QQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAeqyfstlYKTQVRELKEECEEKTKLG 252
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE-------LREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 253 KELQQKKQELQDERDSLAAQLEITLTKADSEQLAR---SIAEEQYSDLEKE-------------------KIMKELEIKE 310
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRqqtevlspeeekelvekikELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 311 MMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKT 390
Cdd:COG1340 154 KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 194387796 391 QAVNKLAEImnRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKL 435
Cdd:COG1340 234 ELQKELREL--RKELKKLRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| C1_Myosin-IXb |
cd20884 |
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ... |
616-677 |
3.96e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410434 Cd Length: 58 Bit Score: 36.38 E-value: 3.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194387796 616 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHKDHMDKkeeIIAPCKVYY 677
Cdd:cd20884 3 YNGHVFTSYQVNIMQSCEQCSSYIWAMEK---ALLCSVCKMTCHKKCLSK---IQSHCSSTC 58
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-486 |
4.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 317 QELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDeeisAAAIKAQFEKQLLTERTLKtQAVNKL 396
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELA-ELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 397 AEIMNRKEPVKRgNDTDVRRKEKENRKLHMELKSEREKLT----QQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDS 472
Cdd:COG4717 149 EELEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....
gi 194387796 473 DIEQLRSQLQALHI 486
Cdd:COG4717 228 ELEQLENELEAAAL 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
12-311 |
4.64e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 12 DLKNGKILLAKVELEKRQLQERFTDLEKEKsnmeidmtyqLKVIQqsleqeeaehkatkarladknkiyesieeAKSEAM 91
Cdd:pfam15921 605 ELQEFKILKDKKDAKIRELEARVSDLELEK----------VKLVN-----------------------------AGSERL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 92 KEMekklleeRTLKQKVENLLLEaekrcslldcdLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKrclTQNDLKMQ 171
Cdd:pfam15921 646 RAV-------KDIKQERDQLLNE-----------VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK---LKMQLKSA 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 172 TQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQL---EAEQYFSTLYKTQV-RELKEECEE 247
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMtnaNKEKHFLKEEKNKLsQELSTVATE 784
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194387796 248 KTKLGKELQQKKQELQDERDSLaAQLEITLTKAdSEQLA--RSIAEEQYSDLEKEKIMKELEIKEM 311
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKV-ANMEVALDKA-SLQFAecQDIIQRQEQESVRLKLQHTLDVKEL 848
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
63-369 |
4.76e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 63 EAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQ 139
Cdd:PLN02939 85 ELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLvgmIQNAEKNILLLNQARLQALEDLEKILTE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 140 KDVLNEDVRNLTLKIEQetqkrclTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKE 219
Cdd:PLN02939 165 KEALQGKINILEMRLSE-------TDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENML 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 220 LQDQLEAeqyfstlYKTQVRELKEECEEKTKLGKELQQKKQELQD-ERDSLAAQLEItlTKADSEQLARSIAEEQYSDLE 298
Cdd:PLN02939 238 LKDDIQF-------LKAELIEVAETEERVFKLEKERSLLDASLRElESKFIVAQEDV--SKLSPLQYDCWWEKVENLQDL 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194387796 299 KEKIMKELEIKEMMARHKQELTEK-DATIASLEETNrtltsdVANLANEKEEL-NNKLKDVQEQLSRlKDEEI 369
Cdd:PLN02939 309 LDRATNQVEKAALVLDQNQDLRDKvDKLEASLKEAN------VSKFSSYKVELlQQKLKLLEERLQA-SDHEI 374
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
26-326 |
5.05e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 26 EKRQLQERFTDLEKEKsnmeidmtyqlkviqqslEQEEAEHKATKarladknkiyESIEEAKSEAMKEMEKKLLE-ERTL 104
Cdd:pfam12128 676 RKDSANERLNSLEAQL------------------KQLDKKHQAWL----------EEQKEQKREARTEKQAYWQVvEGAL 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 105 KQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDV-------LNEDVRNLTLKIEQETQKRC-LTQNDLKMQTQQVN 176
Cdd:pfam12128 728 DAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVdpdviakLKREIRTLERKIERIAVRRQeVLRYFDWYQETWLQ 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 177 TLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEaeqyfstlyktqvrelkEECEEKTKLgKELQ 256
Cdd:pfam12128 808 RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQV-----------------RLSENLRGL-RCEM 869
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194387796 257 QKKQELQDERDSLAAQLEITLTKADSEQLARSiaeeqySDLEKEKIMKELE-----IKEMM----ARHKQELTEKDATI 326
Cdd:pfam12128 870 SKLATLKEDANSEQAQGSIGERLAQLEDLKLK------RDYLSESVKKYVEhfknvIADHSgsglAETWESLREEDHYQ 942
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
100-225 |
5.39e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.04 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 100 EERTLKQKVENLLLEAEKrcslLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLK 179
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKEN----LEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLE 757
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 194387796 180 MSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLE 225
Cdd:pfam05911 758 TRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLE 803
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
73-462 |
5.48e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.42 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 73 LADKNKIYESIEEAKSEAM---KEMEKKLLEE-RTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVlNEDVR 148
Cdd:TIGR01612 1199 IAEIEKDKTSLEEVKGINLsygKNLGKLFLEKiDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI-KAEME 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 149 NLTLKIEQETQKRCLTQ-NDLKMQTQQVNTLKMSEKQLKQENnhLMEMKMNLEKQNAELRKERQDADGQMKELQDqleae 227
Cdd:TIGR01612 1278 TFNISHDDDKDHHIISKkHDENISDIREKSLKIIEDFSEESD--INDIKKELQKNLLDAQKHNSDINLYLNEIAN----- 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 228 qYFSTLYKTQVRELKEECEEKTklgKELQQKKQELQDERDslaaqleitltkaDSEQLARSIAEEQYSDLEKEKIMKELE 307
Cdd:TIGR01612 1351 -IYNILKLNKIKKIIDEVKEYT---KEIEENNKNIKDELD-------------KSEKLIKKIKDDINLEECKSKIESTLD 1413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 308 ----------IKEMMARHKQELTEKDATIASLEETNRTLTSDVAN--LANEKEEL------NNKLKDVQEQLSRLKDEEI 369
Cdd:TIGR01612 1414 dkdidecikkIKELKNHILSEESNIDTYFKNADENNENVLLLFKNieMADNKSQHilkikkDNATNDHDFNINELKEHID 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 370 SAAAIKAQFE---KQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKEnrKLHMELKSEREKLTQQMIKYQKEL 446
Cdd:TIGR01612 1494 KSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE--IIIKEIKDAHKKFILEAEKSEQKI 1571
|
410
....*....|....*.
gi 194387796 447 NEMQAQiaeesQIRIE 462
Cdd:TIGR01612 1572 KEIKKE-----KFRIE 1582
|
|
| C1_PKD1_rpt2 |
cd20842 |
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ... |
619-660 |
5.73e-03 |
|
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410392 Cd Length: 94 Bit Score: 36.92 E-value: 5.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHK 660
Cdd:cd20842 35 HTFVIHSYTRPTVCQYCKKLLKGLFR--QGLQCKDCKFNCHK 74
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
134-401 |
6.30e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 134 NELLKQK-DVLNEDVRNLTLKIEQETQKrCLTQNDLKMQTQQVNTLKMSEKQLKQENnHLMEMKmNLEKQNAELRKERQD 212
Cdd:PHA02562 169 DKLNKDKiRELNQQIQTLDMKIDHIQQQ-IKTYNKNIEEQRKKNGENIARKQNKYDE-LVEEAK-TIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 213 ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLG---------KELQQKKQELQDERDSLAAQLEITLTKADSE 283
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 284 QLARSIAEEQysdlekekIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSR 363
Cdd:PHA02562 326 EEIMDEFNEQ--------SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
250 260 270
....*....|....*....|....*....|....*...
gi 194387796 364 LKDEEisaaaIKAQFEKQLLTERTLKTQAVNKLAEIMN 401
Cdd:PHA02562 398 LVKEK-----YHRGIVTDLLKDSGIKASIIKKYIPYFN 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
95-376 |
6.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 95 EKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQ 174
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 175 VNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKE 254
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 255 LQQKKQELQDE--RDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEET 332
Cdd:COG4372 169 LEQELQALSEAeaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 194387796 333 NRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKA 376
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
19-435 |
7.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 19 LLAKVELEK---RQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKaRLADKNKiyeSIEEAKSEAMKEME 95
Cdd:PRK02224 298 LLAEAGLDDadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD-DLEERAE---ELREEAAELESELE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 96 KKLLEERTLKQKVENL---LLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQEtqkrcltQNDLKMQT 172
Cdd:PRK02224 374 EAREAVEDRREEIEELeeeIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA-------RERVEEAE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 173 QQVNTLKMSE-KQLKQENNHL------MEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLyKTQVRELKEEC 245
Cdd:PRK02224 447 ALLEAGKCPEcGQPVEGSPHVetieedRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERL-EERREDLEELI 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 246 EEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKImkelEIKEMMARhKQELTEKDAT 325
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA----ELKERIES-LERIRTLLAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 326 IASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTE---------RTLKTQAVNKL 396
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEyleqveeklDELREERDDLQ 680
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 194387796 397 AEIMNRKEPVKRGNDTDVRRKEKENRKLHME-LKSEREKL 435
Cdd:PRK02224 681 AEIGAVENELEELEELRERREALENRVEALEaLYDEAEEL 720
|
|
| C1_TNS2-like |
cd20826 |
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ... |
617-673 |
7.55e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410376 Cd Length: 52 Bit Score: 35.06 E-value: 7.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 194387796 617 KGHEFIPTLYHFPTNCEACMKPLWHmfkppPALECRRCHIKCHKDHmdkKEEIIAPC 673
Cdd:cd20826 1 KSHSFKEKSFRKPRTCDVCKQIIWN-----EGSSCRVCKYACHRKC---EPKVTAAC 49
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
43-269 |
7.88e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 43 NMEIDM-TYQLKVIQQSLE-----QEEAEhKATKARLADKNKIYES-IEEAKSEAMKEMEkklleertLKQKVENLLLEA 115
Cdd:PHA02562 180 NQQIQTlDMKIDHIQQQIKtynknIEEQR-KKNGENIARKQNKYDElVEEAKTIKAEIEE--------LTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 116 EKRCSlldcDLKQSQQKINELLKQKDVLNEDVRNL---------TLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLK 186
Cdd:PHA02562 251 EDPSA----ALNKLNTAAAKIKSKIEQFQKVIKMYekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 187 QENNHLMEMKMNLEKQNAELRKERQD---ADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQ 263
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSlitLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
....*.
gi 194387796 264 DERDSL 269
Cdd:PHA02562 407 IVTDLL 412
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
254-398 |
7.95e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 254 ELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKqELTEKDATIASLEETN 333
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-KYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194387796 334 rTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAE 398
Cdd:COG1579 93 -ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
309-445 |
7.96e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 309 KEMMARHKQELtekDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEisaAAIKAQFEKQLltertl 388
Cdd:PRK00409 508 KKLIGEDKEKL---NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEA------ 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194387796 389 kTQAVNKL----AEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSErEKLTQQMIKYQKE 445
Cdd:PRK00409 576 -QQAIKEAkkeaDEIIKELRQLQKGGYASVKAHELIEARKRLNKANE-KKEKKKKKQKEKQ 634
|
|
| C1_RASGRP4 |
cd20863 |
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ... |
619-664 |
8.49e-03 |
|
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Pssm-ID: 410413 Cd Length: 57 Bit Score: 35.14 E-value: 8.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 194387796 619 HEFIPTLYHFPTNCEACMKPLWHMFKppPALECRRCHIKCHKDHMD 664
Cdd:cd20863 4 HNFHETTFKKPTFCDSCSGFLWGVTK--QGYRCQDCGINCHKHCKD 47
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
22-361 |
8.89e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 39.28 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 22 KVELEKRQLQERFTDLEKeksnMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSeAMKEMEKKLLEe 101
Cdd:pfam15742 59 KIKAELKQAQQKLLDSTK----MCSSLTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQEKS-RVADAEEKILE- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 102 rtLKQKVENllleAEKRCSLLDCDL--KQSQQKINELLkqkdvlnEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLK 179
Cdd:pfam15742 133 --LQQKLEH----AHKVCLTDTCILekKQLEERIKEAS-------ENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 180 MSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMK---ELQDQLEAEQYFS-TLYKTQVRELKEECEEKTKLGKEL 255
Cdd:pfam15742 200 DKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQQEKeALQEELQQVLKQLDVHVRKYNEKH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 256 QQKKQELQDERDSLAAqlEITLTKADSEQLARSIAE-EQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNR 334
Cdd:pfam15742 280 HHHKAKLRRAKDRLVH--EVEQRDERIKQLENEIGIlQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEELIKNNK 357
|
330 340
....*....|....*....|....*..
gi 194387796 335 TLTSDVANLANEKEELNNKLKDVQEQL 361
Cdd:pfam15742 358 RTISSVQNRVNFLDEENKQLQENTLRL 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
235-485 |
9.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 235 KTQVRELKEECEEKTKlgKELQQKKQELQDERDSLAAQLEITLTKadseqlaRSIAEEQYSDLEkekimkeleikEMMAR 314
Cdd:PRK02224 186 RGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQ-------REQARETRDEAD-----------EVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 315 HKQELTEkdatIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDE-----------EISAAAIKAQFE---- 379
Cdd:PRK02224 246 HEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEErddllaeagldDADAEAVEARREeled 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 380 -----KQLLTERTLKTQAVNKLAEIMnrkepvkRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIA 454
Cdd:PRK02224 322 rdeelRDRLEECRVAAQAHNEEAESL-------REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270
....*....|....*....|....*....|.
gi 194387796 455 EESQIRIELQMTLDSKDSDIEQLRSQLQALH 485
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
234-322 |
9.85e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194387796 234 YKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEqlARSIAEEQYSDLEKEKIMKELEIKEmma 313
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKE--AKKEADEIIKELRQLQKGGYASVKA--- 606
|
....*....
gi 194387796 314 rhkQELTEK 322
Cdd:PRK00409 607 ---HELIEA 612
|
|
| |
