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Conserved domains on  [gi|578810785|ref|XP_006714815|]
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TNFAIP3-interacting protein 1 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
298-529 3.46e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 63.15  E-value: 3.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   298 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 374
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   375 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 454
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578810785   455 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREALRQQKRKAK 529
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSElEELSEELRELESKRS 911
PRK13922 super family cl19252
rod shape-determining protein MreC; Provisional
214-251 1.81e-04

rod shape-determining protein MreC; Provisional


The actual alignment was detected with superfamily member PRK13922:

Pssm-ID: 473155  Cd Length: 276  Bit Score: 43.43  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 578810785 214 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 251
Cdd:PRK13922  73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
Speriolin_N super family cl25501
Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein ...
14-149 1.27e-03

Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein speriolin.


The actual alignment was detected with superfamily member pfam15058:

Pssm-ID: 434426 [Multi-domain]  Cd Length: 196  Bit Score: 40.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   14 GSVPSGEASAAFERLVKENSRLKEKMqgikmlgELLEESQMEATRLRQKAEELV--KDNELLPPPSPSLGSFDPLAELTG 91
Cdd:pfam15058   3 LLTPYEGLRHQIERLVRENEELKKQV-------RLLRENQELKRALGEACAGRCgrQQRGVFLPPVPAYASEPCSPGPGG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785   92 KD-SNVTASPTAPAcPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGP 149
Cdd:pfam15058  76 RAlAPLAGMPDTPQ-QSAEEGSLVDPLTSSLEDLLSGHAPLSQEDCQACQTTDPVAAPP 133
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
298-529 3.46e-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: 63.15  E-value: 3.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   298 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 374
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   375 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 454
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578810785   455 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREALRQQKRKAK 529
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSElEELSEELRELESKRS 911
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
321-531 1.12e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 321 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR----------KLLLAKSKIEMEETDKEQLTAEAKE 390
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqaEEYELLAELARLEQDIARLEERRRE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 391 LRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFE 470
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE--------------EAEAELAEAEEALLEAEAELAEAEE 379
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810785 471 EDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
452-500 3.88e-07

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 48.11  E-value: 3.88e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578810785 452 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:cd09803   34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
328-494 3.73e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 405
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 406 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 473
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
                        170       180
                 ....*....|....*....|.
gi 578810785 474 qrerSDRERMNEEKEELKKQV 494
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
460-502 2.37e-05

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 43.43  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 578810785  460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 502
Cdd:pfam16516  55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
214-251 1.81e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 43.43  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 578810785 214 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 251
Cdd:PRK13922  73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
Speriolin_N pfam15058
Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein ...
14-149 1.27e-03

Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein speriolin.


Pssm-ID: 434426 [Multi-domain]  Cd Length: 196  Bit Score: 40.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   14 GSVPSGEASAAFERLVKENSRLKEKMqgikmlgELLEESQMEATRLRQKAEELV--KDNELLPPPSPSLGSFDPLAELTG 91
Cdd:pfam15058   3 LLTPYEGLRHQIERLVRENEELKKQV-------RLLRENQELKRALGEACAGRCgrQQRGVFLPPVPAYASEPCSPGPGG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785   92 KD-SNVTASPTAPAcPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGP 149
Cdd:pfam15058  76 RAlAPLAGMPDTPQ-QSAEEGSLVDPLTSSLEDLLSGHAPLSQEDCQACQTTDPVAAPP 133
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
315-425 7.18e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   315 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 393
Cdd:smart00935  18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 578810785   394 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 425
Cdd:smart00935  77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
298-529 3.46e-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: 63.15  E-value: 3.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   298 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 374
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   375 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 454
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578810785   455 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREALRQQKRKAK 529
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSElEELSEELRELESKRS 911
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
321-531 1.12e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 321 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR----------KLLLAKSKIEMEETDKEQLTAEAKE 390
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqaEEYELLAELARLEQDIARLEERRRE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 391 LRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFE 470
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE--------------EAEAELAEAEEALLEAEAELAEAEE 379
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810785 471 EDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
193-541 2.13e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 193 RLASKVHKNEQRTSILQTLcEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEgasgrpgspkmegt 272
Cdd:COG1196  226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-------------- 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 273 gkkAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVnkqwdqhfrsmKQQYEQKITELRQKLADLQKQVTDL 352
Cdd:COG1196  291 ---YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE-----------LEELEEELEELEEELEEAEEELEEA 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 353 EAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtp 432
Cdd:COG1196  357 EAELAEAEE---ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-- 431
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 433 psspptafgspegAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 512
Cdd:COG1196  432 -------------ELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
                        330       340
                 ....*....|....*....|....*....
gi 578810785 513 DEEKAREALRQQKRKAKPEYTWRLPCGGV 541
Cdd:COG1196  498 EAEADYEGFLEGVKAALLLAGLRGLAGAV 526
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
335-531 2.58e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 335 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 414
Cdd:COG1196  195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 415 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 494
Cdd:COG1196  275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578810785 495 EKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-536 4.54e-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: 58.62  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 333 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 412
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 413 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 489
Cdd:COG4942   96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578810785 490 LKKQVEKLQaqvtlsnAQLKAFKDEEKAREALRQQKRKAKPEYTWRL 536
Cdd:COG4942  176 LEALLAELE-------EERAALEALKAERQKLLARLEKELAELAAEL 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
329-500 3.07e-08

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: 54.55  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 408
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 409 REYQ--EKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErmnEE 486
Cdd:COG1579   89 KEYEalQKEIESLKRRISDLEDEI---------------LELMERIEELEEELAELEAELAELEAELEEKKAELD---EE 150
                        170
                 ....*....|....
gi 578810785 487 KEELKKQVEKLQAQ 500
Cdd:COG1579  151 LAELEAELEELEAE 164
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-528 8.56e-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: 55.45  E-value: 8.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   335 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 414
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   415 EIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 494
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALAN--------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
                          170       180       190
                   ....*....|....*....|....*....|....
gi 578810785   495 EKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKA 528
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQ 380
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-519 1.23e-07

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: 54.64  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  300 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 369
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  370 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 448
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810785  449 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 519
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
327-524 1.46e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  327 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 403
Cdd:COG4913   247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  404 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 461
Cdd:COG4913   327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578810785  462 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafkdeEKAREALRQQ 524
Cdd:COG4913   396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL------LALRDALAEA 452
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
200-498 3.52e-07

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: 53.52  E-value: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   200 KNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAG 279
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   280 QQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---------------------------- 331
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaaterrl 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   332 ---EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--------LLAKSKIEMEETDKEQLTAE--AKELRQKVKYL 398
Cdd:TIGR02168  841 edlEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerasleeALALLRSELEELSEELRELEskRSELRRELEEL 920
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   399 QDQLSPLTRQREYQEKEIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAGALLRKqelvtqnelLKQQVKIF------- 469
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
                          330       340
                   ....*....|....*....|....*....
gi 578810785   470 EEDFQRERSDRERMNEEKEELKKQVEKLQ 498
Cdd:TIGR02168  992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
452-500 3.88e-07

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 48.11  E-value: 3.88e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578810785 452 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:cd09803   34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
296-500 8.61e-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: 51.30  E-value: 8.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 296 LGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR------- 365
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyr 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 366 -------KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppssppt 438
Cdd:COG4942  116 lgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE---------- 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578810785 439 afgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:COG4942  186 ------------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
190-428 1.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 269
Cdd:COG1196  268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 270 egTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 346
Cdd:COG1196  329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 347 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 423
Cdd:COG1196  407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                 ....*
gi 578810785 424 EEALS 428
Cdd:COG1196  487 AEAAA 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
329-529 1.90e-06

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: 50.83  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 408
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   409 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNEEKE 488
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRA 810
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 578810785   489 ELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAK 529
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
297-524 2.10e-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: 50.84  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   297 GAAEKKVKmLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEM 376
Cdd:TIGR02169  164 GVAEFDRK-KEKALEELEEVEENIER--------LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   377 EETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL-----EEALSIQTppsspptAFGSPEGAGALLR 451
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKE-------KIGELEAEIASLE 307
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578810785   452 KQElvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEekaREALRQQ 524
Cdd:TIGR02169  308 RSI-----AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---LEDLRAE 372
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
328-531 2.59e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 407
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 408 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 486
Cdd:COG3883   92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578810785 487 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
328-494 3.73e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 49.83  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 405
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 406 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 473
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
                        170       180
                 ....*....|....*....|.
gi 578810785 474 qrerSDRERMNEEKEELKKQV 494
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
207-534 1.19e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 207 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgrpgspKMEGTGKKAVAGQQQASVT 286
Cdd:COG4717   43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 287 AGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 366
Cdd:COG4717  115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 367 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 435
Cdd:COG4717  187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 436 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEE 515
Cdd:COG4717  267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
                        330
                 ....*....|....*....
gi 578810785 516 KAREALRQQKRKAKPEYTW 534
Cdd:COG4717  347 EELQELLREAEELEEELQL 365
PTZ00121 PTZ00121
MAEBL; Provisional
191-527 1.49e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  191 FNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENlELKKLLMSNGNKEGASGRpgspKME 270
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKK----KAE 1339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  271 GTGKKAVAGQQQASVTAGKvpevvaLGAAEKKVKMLEQQRSElleVNKQWDQHFRsmKQQYEQKITELRQKLADLQKQVT 350
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKEE---AKKKADAAKK--KAEEKKKADEAKKKAEEDKKKAD 1408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  351 DLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKylQDQLSPLTRQREYQEKEIQRLNKALEEAlsiq 430
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEA---- 1482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  431 tppsspPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQVTLSNAQ 507
Cdd:PTZ00121 1483 ------KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEE 1556
                         330       340
                  ....*....|....*....|
gi 578810785  508 LKAFKDEEKAREALRQQKRK 527
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDK 1576
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-531 1.53e-05

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: 48.14  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgr 263
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL------------- 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   264 pgspkmegTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEqqRSELLEVNKQWDQHFRSMKQQY---EQKITELRQ 340
Cdd:TIGR02169  750 --------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVsriEARLREIEQ 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   341 KLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQ 417
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   418 RLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSD-RERMNEEK--EELKKQ 493
Cdd:TIGR02169  900 ELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIpEEELSLEDvqAELQRV 963
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 578810785   494 VEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:TIGR02169  964 EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-497 1.64e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  292 EVVALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLL 368
Cdd:COG4913   659 DEIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  369 LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGA 446
Cdd:COG4913   735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESL 814
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578810785  447 GALLRKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 497
Cdd:COG4913   815 PEYLALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
332-533 1.88e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  332 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 403
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  404 PLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 483
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIG------------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578810785  484 NEEKEELKKQV-EKLQAQVTLSNAQLkafkdeEKAREALRQQKRKAKPEYT 533
Cdd:COG4913   757 AALGDAVERELrENLEERIDALRARL------NRAEEELERAMRAFNREWP 801
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
460-502 2.37e-05

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 43.43  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 578810785  460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 502
Cdd:pfam16516  55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-494 2.93e-05

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: 46.98  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegaSGR 263
Cdd:TIGR02169  718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL----------EAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   264 PGSPKMEGTGKKAVAGQQQASVTAGKVPEV-VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 339
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   340 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 419
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   420 NKALEEalsIQTPPSSPPTAFGSPEGAGALLRKQELV-------------TQNELLKQQVKIFEEdfqreRSDRERMNEE 486
Cdd:TIGR02169  940 KGEDEE---IPEEELSLEDVQAELQRVEEEIRALEPVnmlaiqeyeevlkRLDELKEKRAKLEEE-----RKAILERIEE 1011

                   ....*...
gi 578810785   487 KEELKKQV 494
Cdd:TIGR02169 1012 YEKKKREV 1019
PTZ00121 PTZ00121
MAEBL; Provisional
195-529 4.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  195 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGT 272
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  273 GKKAVAGQQQASVTAGKVPEvvALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQKlADLQKQV 349
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKA-AEAKKKA 1512
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  350 TDLEAEREQKQRDFDRKlllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 429
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKK---AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA 1589
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  430 QTPPSSPPTAFGSPEG---------AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE--LKKQVEKLQ 498
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKkmkaeeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkIKAAEEAKK 1669
                         330       340       350
                  ....*....|....*....|....*....|.
gi 578810785  499 AQVTLSNAQlKAFKDEEKAREALRQQKRKAK 529
Cdd:PTZ00121 1670 AEEDKKKAE-EAKKAEEDEKKAAEALKKEAE 1699
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
300-532 6.20e-05

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: 45.88  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  300 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 379
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  380 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 455
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  456 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREALRQ- 523
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQi 581
                         250
                  ....*....|
gi 578810785  524 -QKRKAKPEY 532
Cdd:pfam17380 582 vESEKARAEY 591
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
299-529 1.02e-04

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: 45.44  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   299 AEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AEREQKQRDFDRKLLLAKSKIE 375
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKERELEDAEERLAKLEAEID 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   376 MEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqel 455
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------------------------ 382
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785   456 vTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREALRQQKRKAK 529
Cdd:TIGR02169  383 -TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkEDKALEIKKQEWKLE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-430 1.28e-04

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: 45.05  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 269
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL------------------- 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   270 egtgkKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 349
Cdd:TIGR02168  350 -----KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   350 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 428
Cdd:TIGR02168  417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496

                   ..
gi 578810785   429 IQ 430
Cdd:TIGR02168  497 LQ 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
315-528 1.52e-04

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: 44.66  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   315 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 392
Cdd:TIGR02168  197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   393 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 469
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785   470 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKA 528
Cdd:TIGR02168  347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
PTZ00121 PTZ00121
MAEBL; Provisional
186-531 1.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  186 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRP 264
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  265 GSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 339
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  340 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 416
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  417 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNELLK----QQVKIFEEDFQRERSDR---ERMNEEKEE 489
Cdd:PTZ00121 1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKikaEEAKKEAEE 1741
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 578810785  490 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
214-251 1.81e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 43.43  E-value: 1.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 578810785 214 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 251
Cdd:PRK13922  73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
PRK12704 PRK12704
phosphodiesterase; Provisional
289-419 1.99e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 289 KVPEVVALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 360
Cdd:PRK12704  27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785 361 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 419
Cdd:PRK12704  96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
295-399 2.83e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 43.04  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  295 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 367
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578810785  368 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 399
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
282-384 2.97e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.79  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  282 QASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 361
Cdd:PRK11448  140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
                          90       100
                  ....*....|....*....|...
gi 578810785  362 DFDRKlllAKSKIEMEETDKEQL 384
Cdd:PRK11448  220 EITDQ---AAKRLELSEEETRIL 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
190-449 3.89e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgrpgspKM 269
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 270 EGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 349
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 350 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 429
Cdd:COG4942  167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
                        250       260
                 ....*....|....*....|
gi 578810785 430 QTPPSSPPTAFGSPEGAGAL 449
Cdd:COG4942  236 AAAAAERTPAAGFAALKGKL 255
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-514 3.91e-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: 43.47  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  300 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 379
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  380 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 459
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578810785  460 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 514
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
321-529 4.13e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 321 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREqkqrDFDRKLLLAkskiemeetdkeQLTAEAKELRQKVKYLQD 400
Cdd:COG3206  163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALE----EFRQKNGLV------------DLSEEAKLLLQQLSELES 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 401 QLSPLTRQREYQEKEIQRLNKALEEAlsiqtpPSSPPTAFGSPEGAGALLRKQELVTQnelLKQQVKIFEEDFQRERSDR 480
Cdd:COG3206  227 QLAEARAELAEAEARLAALRAQLGSG------PDALPELLQSPVIQQLRAQLAELEAE---LAELSARYTPNHPDVIALR 297
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578810785 481 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAfkDEEKAREALRQQKRKAK 529
Cdd:COG3206  298 AQIAALRAQLQQEAQRILASLEAELEALQA--REASLQAQLAQLEARLA 344
mukB PRK04863
chromosome partition protein MukB;
310-513 4.15e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  310 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 389
Cdd:PRK04863  491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  390 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 464
Cdd:PRK04863  562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578810785  465 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 513
Cdd:PRK04863  635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
184-500 4.66e-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: 43.42  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGR 263
Cdd:pfam02463  675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   264 PGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 343
Cdd:pfam02463  755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   344 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 413
Cdd:pfam02463  835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   414 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 477
Cdd:pfam02463  915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
                          330       340
                   ....*....|....*....|...
gi 578810785   478 SDRERMNEEKEELKKQVEKLQAQ 500
Cdd:pfam02463  995 LEKERLEEEKKKLIRAIIEETCQ 1017
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
306-524 5.61e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 306 LEQQRSELLEVNKQWDQhfrsmKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQ 383
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERREE 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 384 LTaeakELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSpPTAFGSPEGAGALLRKQELVTQNELLK 463
Cdd:PRK02224 253 LE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA-EAGLDDADAEAVEARREELEDRDEELR 327
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810785 464 Q-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafKDEEKAREALRQQ 524
Cdd:PRK02224 328 DrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---EDRREEIEELEEE 392
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
190-509 8.80e-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: 42.41  E-value: 8.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   190 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGS 266
Cdd:pfam15921  518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   267 P---------------KMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 328
Cdd:pfam15921  594 QlekeindrrlelqefKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 395
Cdd:pfam15921  674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   396 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 475
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 578810785   476 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 509
Cdd:pfam15921  821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
306-427 1.14e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 306 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 385
Cdd:COG0542  413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 386 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 427
Cdd:COG0542  492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
213-523 1.20e-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: 42.13  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   213 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAG---- 288
Cdd:pfam12128  322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGikdk 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   289 --KVPEVVALGAAEKKvKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLAdlqkQVTDLEAEREQKqrdfdrk 366
Cdd:pfam12128  399 laKIREARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLN----QATATPELLLQL------- 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   367 lllAKSKIEMEETDKEQLTAEAKELRqkvkyLQDQLSPLTRQREYQEKEIQRLNK-------ALEEALSIQTPPSSPPTA 439
Cdd:pfam12128  467 ---ENFDERIERAREEQEAANAEVER-----LQSELRQARKRRDQASEALRQASRrleerqsALDELELQLFPQAGTLLH 538
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   440 FGSPEGAG-----------ALLRKQEL------------------------------VTQNELLKQQVKIFEEDFQRERS 478
Cdd:pfam12128  539 FLRKEAPDweqsigkvispELLHRTDLdpevwdgsvggelnlygvkldlkridvpewAASEEELRERLDKAEEALQSARE 618
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 578810785   479 DRERMNEEKEELKKQVEKLQAQVTLSNAQLKafkdeeKAREALRQ 523
Cdd:pfam12128  619 KQAAAEEQLVQANGELEKASREETFARTALK------NARLDLRR 657
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
186-500 1.23e-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: 41.65  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  186 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkLLMSNGNKEGASGRPG 265
Cdd:pfam17380 341 RMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE------LEAARKVKILEEERQR 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  266 SPKMEGTGKKAVAGQQQAsvtagkvpevvalgAAEKKVKMLEQQRSELLEvnkqwdqHFRSMKQQYEQKITELRQKLADL 345
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEE--------------ARQREVRRLEEERAREME-------RVRLEEQERQQQVERLRQQEEER 472
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  346 QKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREYQEKEIQRLNKALEE 425
Cdd:pfam17380 473 KRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKLLEKEMEERQKAIYE 531
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578810785  426 ALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:pfam17380 532 EERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
Speriolin_N pfam15058
Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein ...
14-149 1.27e-03

Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein speriolin.


Pssm-ID: 434426 [Multi-domain]  Cd Length: 196  Bit Score: 40.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   14 GSVPSGEASAAFERLVKENSRLKEKMqgikmlgELLEESQMEATRLRQKAEELV--KDNELLPPPSPSLGSFDPLAELTG 91
Cdd:pfam15058   3 LLTPYEGLRHQIERLVRENEELKKQV-------RLLRENQELKRALGEACAGRCgrQQRGVFLPPVPAYASEPCSPGPGG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578810785   92 KD-SNVTASPTAPAcPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGP 149
Cdd:pfam15058  76 RAlAPLAGMPDTPQ-QSAEEGSLVDPLTSSLEDLLSGHAPLSQEDCQACQTTDPVAAPP 133
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
142-516 1.42e-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: 41.64  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   142 ANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDhgqlfthlGRMALEFNRLASKVHKNEQRTSI---LQTLCEQLRKE 218
Cdd:pfam15921  409 GNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKV 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   219 NEALKAKlDKGLEQRDQAAERLrEENLELKKLLMSNGNKEGASGRPGSP-KMEGTGKKAVAGQQQASVTAGKVPEVVALG 297
Cdd:pfam15921  481 VEELTAK-KMTLESSERTVSDL-TASLQEKERAIEATNAEITKLRSRVDlKLQELQHLKNEGDHLRNVQTECEALKLQMA 558
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   298 AAEKKVKMLEQQRSELLEVNKQWDQHFRSM---KQQYEQKITELR--------------QKLADLQKQVTDLEAEReQKQ 360
Cdd:pfam15921  559 EKDKVIEILRQQIENMTQLVGQHGRTAGAMqveKAQLEKEINDRRlelqefkilkdkkdAKIRELEARVSDLELEK-VKL 637
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   361 RDFDRKLLLAKSKIEMEetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SIQTPPSSPPTA 439
Cdd:pfam15921  638 VNAGSERLRAVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSAQSELEQTRNT 714
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   440 FGSPEGAGALLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 510
Cdd:pfam15921  715 LKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV 794

                   ....*.
gi 578810785   511 FKDEEK 516
Cdd:pfam15921  795 LRSQER 800
46 PHA02562
endonuclease subunit; Provisional
294-532 1.79e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 294 VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSK 373
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAK 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 374 IEMEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspp 437
Cdd:PHA02562 267 IKSK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK------ 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 438 tafgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKA 517
Cdd:PHA02562 338 -------------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                        250
                 ....*....|....*
gi 578810785 518 REALRQQKRKAKPEY 532
Cdd:PHA02562 391 IVKTKSELVKEKYHR 405
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
268-515 1.83e-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: 41.26  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   268 KMEGTGKKAVAGQQQASVTAGKVpEVVAlGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQK------ 341
Cdd:pfam15921  279 EITGLTEKASSARSQANSIQSQL-EIIQ-EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlans 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   342 --------------------------LADLQKQVTDLEAEREQKQRDFDRKLllaKSKIEMEETDKEqLTAEAKELRQKV 395
Cdd:pfam15921  357 eltearterdqfsqesgnlddqlqklLADLHKREKELSLEKEQNKRLWDRDT---GNSITIDHLRRE-LDDRNMEVQRLE 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   396 KYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafGSPEGAGALLRK--QELVTQnellkqqvKIFEEDF 473
Cdd:pfam15921  433 ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT----------AQLESTKEMLRKvvEELTAK--------KMTLESS 494
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 578810785   474 QRERSDRERMNEEKEE----LKKQVEKLQAQVTLSNAQLKAFKDEE 515
Cdd:pfam15921  495 ERTVSDLTASLQEKERaieaTNAEITKLRSRVDLKLQELQHLKNEG 540
PTZ00121 PTZ00121
MAEBL; Provisional
213-487 1.87e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  213 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPE 292
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  293 VVALGAAEKKVKMLEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 372
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  373 KIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagalL 450
Cdd:PTZ00121 1701 AKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH------------------L 1762
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578810785  451 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 487
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
304-426 2.17e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 304 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 383
Cdd:COG2433  384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 578810785 384 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 426
Cdd:COG2433  450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-500 2.33e-03

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: 40.77  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  300 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLqKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET 379
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  380 DKEQLTAEAKELRQKVKYLQDQLSpltrqREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQelvtqn 459
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQK----------------SLKKKQ------ 584
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 578810785  460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
PRK11281 PRK11281
mechanosensitive channel MscK;
329-525 2.65e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDKEQL-TAEAKELRQKVKYLQDQLspltr 407
Cdd:PRK11281   69 LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETRETLsTLSLRQLESRLAQTLDQL----- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  408 qreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FGSPEGAGALL--RKQELVTQNELLKQQV 466
Cdd:PRK11281  138 ---------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKGGKVGGKALRpsQRVLLQAEQALLNAQN 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578810785  467 kifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQLKAFkdEEKAREALRQQK 525
Cdd:PRK11281  209 -----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKRLTLS--EKTVQEAQSQDE 270
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
329-529 3.62e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.42  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  329 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 398
Cdd:PRK10929   68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  399 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 477
Cdd:PRK10929  136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578810785  478 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREALRQQKRKAK 529
Cdd:PRK10929  200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAE 251
PRK11281 PRK11281
mechanosensitive channel MscK;
213-485 3.70e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  213 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgrpgspkmegtgkkAVAGQQQASVTAgkvpE 292
Cdd:PRK11281   52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  293 VVALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 359
Cdd:PRK11281  103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  360 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 424
Cdd:PRK11281  168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578810785  425 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 485
Cdd:PRK11281  248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
193-533 3.95e-03

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: 40.34  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   193 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGT 272
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   273 GKKAvagqqqasvtagkvpevvalgAAEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 352
Cdd:pfam02463  254 ESSK---------------------QEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   353 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 432
Cdd:pfam02463  310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   433 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 512
Cdd:pfam02463  386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
                          330       340
                   ....*....|....*....|.
gi 578810785   513 DEEKAREALRQQKRKAKPEYT 533
Cdd:pfam02463  465 LELKKSEDLLKETQLVKLQEQ 485
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-531 4.38e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 332 EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEEtDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY 411
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKELKEK 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 412 qEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKifeeDFQRERSDRERMNEEKEELK 491
Cdd:PRK03918 292 -AEEYIKLSEFYEEYLD----------------------ELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELK 344
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 578810785 492 KQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKPE 531
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL 384
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
296-426 4.54e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 296 LGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVTDLEAEREQKQRdfdR 365
Cdd:COG3206  242 LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQ---R 313
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578810785 366 KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 426
Cdd:COG3206  314 ILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
321-529 5.45e-03

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: 39.62  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  321 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK-------IEMEETDKEQLTAEAKELRQ 393
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnqlKDEQNKIKKQLSEKQKELEQ 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  394 ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegagallRKQELVTQNEL------- 461
Cdd:TIGR04523 279 nnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ--------------------EKKLEEIQNQIsqnnkii 337
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  462 --LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlSNAQLKAFKDEEKAREALRQQKRKAK 529
Cdd:TIGR04523 338 sqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESKIQNQE 404
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
298-399 5.56e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 298 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 377
Cdd:cd16269  202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
                         90       100
                 ....*....|....*....|..
gi 578810785 378 ETDKEQLTAEAKELRQKVKYLQ 399
Cdd:cd16269  270 ALLEEGFKEQAELLQEEIRSLK 291
Filament pfam00038
Intermediate filament protein;
302-424 5.99e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 39.13  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  302 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 377
Cdd:pfam00038  19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578810785  378 ETDKEQLTAEAKELRQkvkylqdQLSPLTRQREYQEKEIQRLNKALE 424
Cdd:pfam00038  95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
213-522 6.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 213 EQLRKENEALKAKLDKGLEQRDQAAERLrEENLElkkllmsngNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPE 292
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFL-EELRE---------ERDELREREAELEATLRTARERVEEAEALLEAGKCPE 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 293 ----------VVALGAAEKKVKMLEQQRSEL-LEVNKQWDQHFRSMK-QQYEQKITELRQKLADLQKQVTD----LEAER 356
Cdd:PRK02224 457 cgqpvegsphVETIEEDRERVEELEAELEDLeEEVEEVEERLERAEDlVEAEDRIERLEERREDLEELIAErretIEEKR 536
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 357 EQKQRDFDRKLLLAKSKIEMEETDKEQlTAEAKELRQKVKYLQDQLSPLTRQREYQEK-------------EIQRLNKAL 423
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEA-EEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKR 615
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 424 EEALSIQTppsspptafgspegagalLRKQELVTQNELLKQQVKIFEED-FQRERSDRERMNEEKEELKKQVEKLQAQVT 502
Cdd:PRK02224 616 EALAELND------------------ERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERD 677
                        330       340
                 ....*....|....*....|
gi 578810785 503 LSNAQLKAFKDEEKAREALR 522
Cdd:PRK02224 678 DLQAEIGAVENELEELEELR 697
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-496 7.17e-03

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: 39.23  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  300 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAE---REQKQRDFDRKLL-----LAK 371
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEKLESEkkeKESKISDLEDELNkddfeLKK 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  372 SKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppsspptaf 440
Cdd:TIGR04523 557 ENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA-------------- 622
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578810785  441 gSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 496
Cdd:TIGR04523 623 -KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
315-425 7.18e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785   315 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 393
Cdd:smart00935  18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 578810785   394 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 425
Cdd:smart00935  77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
384-504 7.67e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 38.59  E-value: 7.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785  384 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 462
Cdd:pfam09787  45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 578810785  463 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 504
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
196-448 8.20e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 196 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGRPGSPKMEGTGKK 275
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 276 AVAGQQQASVTAGKVPEVV-------ALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 348
Cdd:COG3883   91 RARALYRSGGSVSYLDVLLgsesfsdFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578810785 349 VTDLEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 428
Cdd:COG3883  163 KAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
                        250       260
                 ....*....|....*....|
gi 578810785 429 IQTPPSSPPTAFGSPEGAGA 448
Cdd:COG3883  225 AAAAAAAAAAAAAAAAAAAA 244
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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