|
Name |
Accession |
Description |
Interval |
E-value |
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
412-508 |
1.34e-23 |
|
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: 95.44 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 412 EELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 491
Cdd:pfam16516 1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80
|
90
....*....|....*..
gi 1938958523 492 EKEQLALQLAILLKENN 508
Cdd:pfam16516 81 EKEQLAAQLEYLQRQNQ 97
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
425-511 |
5.06e-23 |
|
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: 93.18 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 425 VQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILL 504
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 1938958523 505 KENNDFE 511
Cdd:cd09803 81 RENQELK 87
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
37-103 |
5.07e-18 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 78.29 E-value: 5.07e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958523 37 PEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHE 103
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
559-584 |
1.37e-13 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 64.53 E-value: 1.37e-13
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-466 |
4.87e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 133 RTDLEQEVEQLKRQVEQ--------------EVEHLKNQVRRLQAEKADLLGIVSELQLKLNssgssedsfvEIRMTEGE 198
Cdd:COG1196 195 LGELERQLEPLERQAEKaeryrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELE----------ELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 199 AEGAMKEMRNSagptrtdsismgkctedartcVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKanghsA 278
Cdd:COG1196 265 LEAELEELRLE---------------------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 279 IETQTEGSTQKEEEDKDPEsvgiEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQEL 358
Cdd:COG1196 319 EELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 359 VYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTI--EELTKQQAEKVDKVQLQELSEKLEL 436
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAaeEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350
....*....|....*....|....*....|
gi 1938958523 437 AEQALASKQLQMDEMKQTIAKQEEDLETMA 466
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
245-462 |
1.33e-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: 54.68 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 245 LREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEED-----KDPESVGIEVETLNVQVASLFKELQE 319
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqleERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 320 AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQElVYSNRKLELQveSMRSEIKMEQAKTEEEKSRLATLQATHDK 399
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938958523 400 LLQEHNKALRTIEELTKQQAEKVDkvQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDL 462
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELES--ELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-467 |
4.69e-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: 53.14 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 225 EDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKdpESVGIEVE 304
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 305 TLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELnekQELVYSNRKLELQVESMRSEIKMEQAKTE 384
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL---EDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 385 EEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQ-----LQELSEKLELAEQALASKQLQMDEMKQTIAKQE 459
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSelrreLEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
....*...
gi 1938958523 460 EDLETMAV 467
Cdd:TIGR02168 950 SLTLEEAE 957
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
38-509 |
5.70e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLK---EAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLK--EELG 112
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 113 KLKEKSERPFEDITgrcgfPRTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEI 192
Cdd:PTZ00121 1398 KKAEEDKKKADELK-----KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 193 RMTEGEAEGAMK--EMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFE 270
Cdd:PTZ00121 1473 DEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 271 KKANGHSAIETQTEGSTQKEEEDKDP----------------ESVGIEVETLNVQVASLFKELQEAHTKLSEA----ELM 330
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMalrkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaeEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 331 KKRLQEKCQALERKNSAtpsELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQathdklLQEHNKALRT 410
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKA---EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA------LKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 411 IEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMK-QTIAKQEEDLETMAVLRAQMEVYCSDFHAERAA--RE 487
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEE 1783
|
490 500
....*....|....*....|..
gi 1938958523 488 KIHEEKEQLALQLAILLKENND 509
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
245-506 |
2.08e-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: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 245 LREGNQKVERLEIAL-----REAKERISDFEKKANghSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQE 319
Cdd:TIGR02168 215 YKELKAELRELELALlvlrlEELREELEELQEELK--EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 320 AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQElvySNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQAthdk 399
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEELEA---- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 400 LLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKlelAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDF 479
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
250 260
....*....|....*....|....*..
gi 1938958523 480 HAERAAREKIHEEKEQLALQLAILLKE 506
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREE 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-420 |
4.75e-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: 49.68 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMklnnQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEK 117
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 118 SERPFEDITgrcgfprtDLEQEVEQLKRQV-EQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTE 196
Cdd:TIGR02169 767 IEELEEDLH--------KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 197 GEAEGAMKEMRNSagptrtdsismgkctedartcvefEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGH 276
Cdd:TIGR02169 839 QEQRIDLKEQIKS------------------------IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 277 SAietqtegstQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEkcqalerknsaTPSELNEKQ 356
Cdd:TIGR02169 895 EA---------QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-----------IPEEELSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938958523 357 ELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAE 420
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-461 |
8.59e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 78 KQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKNQ 157
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 158 VRRLQAEKAdllgivselqlklnsSGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELT 237
Cdd:PTZ00121 1287 EEKKKADEA---------------KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 238 VSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGhsaiETQTEGSTQKEEEDKDPEsvgievetlnvqvaslfKEL 317
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE----KKKADEAKKKAEEDKKKA-----------------DEL 1410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 318 QEAHTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATH 397
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1938958523 398 DKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEED 461
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-461 |
2.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 249 NQKVERLEIALREAKERISDFeKKANGHSAIETQTEGSTQKeeedkdpesvgieVETLNVQVASLFKELQEAHTKLSEAE 328
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-RQKNGLVDLSEEAKLLLQQ-------------LSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 329 LMKKRLQEKC---------QALERKNSATPSELNEKQELVYSN----RKLELQVESMRSEIKMEQAKTEEE-KSRLATLQ 394
Cdd:COG3206 247 AQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASlEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958523 395 ATHDKLLQEHNKALRTIEELTKQQaekvdkVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEED 461
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELE------AELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-494 |
2.97e-05 |
|
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: 47.36 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMKLNNQAMKGRFEEL-SAWTEKQKE-----------ERQLFEIQSK--EAKERLKALSHE 103
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELeSRLEELEEQletlrskvaqlELQIASLNNEieRLEARLERLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 104 NERLKEELGKL-KEKSERPFEDITGRCGFPRTDLEQEVEQLkRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSS 182
Cdd:TIGR02168 416 RERLQQEIEELlKKLEEAELKELQAELEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 183 GSSEDSFveirmtEGEAEGAMKEMRNSAG-----PTRTDSISMGK-----------------CTED---ARTCVEF---- 233
Cdd:TIGR02168 495 ERLQENL------EGFSEGVKALLKNQSGlsgilGVLSELISVDEgyeaaieaalggrlqavVVENlnaAKKAIAFlkqn 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 234 EELTVSQLLLCLREGNQK-----------------------------------------VERLEIALREAK-----ERI- 266
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIqgndreilkniegflgvakdlvkfdpklrkalsyllggvlvVDDLDNALELAKklrpgYRIv 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 267 ----------------------SDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKL 324
Cdd:TIGR02168 649 tldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 325 SEAELMKKRLQEKCQALERKNSATPSELNEKQElvysnrklelQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEH 404
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEA----------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 405 NKALRTIEELtkQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERA 484
Cdd:TIGR02168 799 KALREALDEL--RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
570
....*....|
gi 1938958523 485 AREKIHEEKE 494
Cdd:TIGR02168 877 ALLNERASLE 886
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-506 |
3.22e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 254 RLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDpesvgiEVETLNVQVASLFKELQEAHTKLSEAELMKKR 333
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA------ELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 334 LQEKCQALERKNSATPSEL----NEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALR 409
Cdd:COG1196 300 LEQDIARLEERRRELEERLeeleEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 410 TIEELTKQQAEKVDkvQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEvycSDFHAERAAREKI 489
Cdd:COG1196 380 ELEELAEELLEALR--AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE---EALEEAAEEEAEL 454
|
250
....*....|....*..
gi 1938958523 490 HEEKEQLALQLAILLKE 506
Cdd:COG1196 455 EEEEEALLELLAELLEE 471
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-520 |
4.39e-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: 46.60 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 133 RTDLEQEVEQLKRqVEQEVEHLKNQVRRLQAEKADLLgivselqlklnssgssedSFVEIRMTEGEAEGamKEMRNSAGP 212
Cdd:TIGR02169 176 LEELEEVEENIER-LDLIIDEKRQQLERLRREREKAE------------------RYQALLKEKREYEG--YELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 213 TRTDSISMGKCTEDARTcvEFEELTVSqlllcLREGNQKVERLEIALREAKERISDfekkanghsaietqtEGSTQKEEE 292
Cdd:TIGR02169 235 LERQKEAIERQLASLEE--ELEKLTEE-----ISELEKRLEEIEQLLEELNKKIKD---------------LGEEEQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 293 DKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERknsatpsELNEKQELVysnRKLELQVESM 372
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRR---DKLTEEYAEL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 373 RSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQ-----LQELSEKLELAEQALASKQLQ 447
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQrlseeLADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938958523 448 MDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLM 520
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-506 |
5.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 50 ENHQLKEAMKLNNQAMKGrfEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPfeditgrc 129
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-------- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 130 GFPRTDLEQEVEQLKRQVEQ--EVEHLKNQVRRLQaEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMK--E 205
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKadE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 206 MRNSAGPTRTDSiSMGKCTEDARTCVEF-----EELTVSQLLLCLREGNQKVERLEIAlREAKERISDFEKKANGHSAIE 280
Cdd:PTZ00121 1449 AKKKAEEAKKAE-EAKKKAEEAKKADEAkkkaeEAKKADEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 281 TQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAE--LMKKRLQEKCQALERKNSATPSELNEKQEl 358
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEVMKLYEEEK- 1605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 359 vysNRKLELQVESMRSEIKMEQAKTEEEKSR----LATLQATHDKLLQEHNKA-----LRTIEELTKQQAEKVDKVQLQE 429
Cdd:PTZ00121 1606 ---KMKAEEAKKAEEAKIKAEELKKAEEEKKkveqLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAEEDKKKAEEAKK 1682
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1938958523 430 LSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVycSDFHAERAAREKIHEEKEQLALQLAILLKE 506
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
71-471 |
5.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 71 ELSAWTEKQKEERqlfeIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGrCGFPRTDLEQEVEQLKRQVEQ- 149
Cdd:PRK02224 217 ELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAE-TEREREELAEEVRDLRERLEEl 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 150 --EVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSS-EDSFVEIRMTEGEAEGA---MKEMRNSAGPTRTDSISMGKC 223
Cdd:PRK02224 292 eeERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQAHNEEAESLredADDLEERAEELREEAAELESE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 224 TEDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEED---------- 293
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERveeaeallea 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 294 -KDPE----------------------SVGIEVETLNVQVASLFKELQEAhTKLSEAELMKKRLQEKCQALERKNSATPS 350
Cdd:PRK02224 452 gKCPEcgqpvegsphvetieedrerveELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 351 ELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQ-LQE 429
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDeIER 610
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1938958523 430 LSEKLE-LAEQALASKQlQMDEMKQTIAKQEEDLETMAVLRAQ 471
Cdd:PRK02224 611 LREKREaLAELNDERRE-RLAEKRERKRELEAEFDEARIEEAR 652
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
225-463 |
7.52e-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: 45.83 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 225 EDARTCVEFEELTVSQLLLCLREGNQKVERLEIAlREAKERISDFEKKAnghsaIET-QTEGSTQKEEEDKdpesvgiEV 303
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEK-----REYeGYELLKEKEALER-------QK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 304 ETLNVQVASLFKELQEAHTKLSEAElmkKRLQEKCQALErknsatpsELNEKQELVYSNRKLELQ--VESMRSEIKMEQA 381
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELE---KRLEEIEQLLE--------ELNKKIKDLGEEEQLRVKekIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 382 KTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAE-KVDKVQLQE----LSEKLELAEQALASKQLQMDEMKQTIA 456
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEeRKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELK 388
|
....*..
gi 1938958523 457 KQEEDLE 463
Cdd:TIGR02169 389 DYREKLE 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-460 |
1.54e-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: 44.37 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 241 LLLCLREGNQKVERLEIALREAKERISDFEKKANghSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEA 320
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELA--ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 321 HTKLSEAEL----MKKRLQEKCQALERKNSATPSEL----NEKQELVYSNRKLELQVESMRS---EIKMEQAKTEEEKSR 389
Cdd:COG4942 89 EKEIAELRAeleaQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1938958523 390 LATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQ--MDEMKQTIAKQEE 460
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEalIARLEAEAAAAAE 241
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
327-441 |
1.68e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 327 AELMKKRLQEKCQALERKNSATPSELNEKQELVysnRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNK 406
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI---RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1938958523 407 ALRTIEELTKQQAE------KVDKVQ--LQELSEKLELAEQAL 441
Cdd:COG2433 460 EIRKDREISRLDREierlerELEEERerIEELKRKLERLKELW 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
82-494 |
1.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 82 ERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFE------DITGRCGFPR---TDLEQEVEQL---KRQVEQ 149
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQAREtrdeadEVLEEHEERReelETLEAEIEDLretIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 150 EVEHLKNQVRRLQAEKADLL----GIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMgkcTE 225
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEeerdDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL---RE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 226 DARTCVEFEELTVSQlllcLREGNQKVERLEIALREAKERISDFEKKANghSAIETQTEGSTQKEEEDKDPESVGIEVET 305
Cdd:PRK02224 350 DADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIE--ELRERFGDAPVDLGNAEDFLEELREERDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 306 LNVQVASLFKELQEAHTKLSEAElmkkRLQE--KCQALER--KNSATPSELNEKQElvysnRKLELQVEsmRSEIKMEQA 381
Cdd:PRK02224 424 LREREAELEATLRTARERVEEAE----ALLEagKCPECGQpvEGSPHVETIEEDRE-----RVEELEAE--LEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 382 KTEEEKSRLATLQATHDKLLQEHNKAlRTIEELTKQQAEKVDKVQLQ---------ELSEKLELAEQALASKQLQMDEMK 452
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERaeelreraaELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1938958523 453 QTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKE 494
Cdd:PRK02224 572 EEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
77-493 |
1.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 77 EKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERpFEDITGRcgfpRTDLEQEVEQLKRQVE--QEVEHL 154
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-LEELKKK----LKELEKRLEELEERHElyEEAKAK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 155 KNQVRRLQAEKADLL--GIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTdsiSMGKCTEDARTCVE 232
Cdd:PRK03918 371 KEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK---AKGKCPVCGRELTE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 233 FEELTV-SQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIE--------V 303
Cdd:PRK03918 448 EHRKELlEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEelekkaeeY 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 304 ETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRK-LELQVESMRS------EI 376
Cdd:PRK03918 528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELEPfyneylEL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 377 KMEQAKTEEEKSRLATLQATHDKL---LQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQM----- 448
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEELDKAfeeLAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELeelek 687
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1938958523 449 --DEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEK 493
Cdd:PRK03918 688 rrEEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
38-443 |
2.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMKlNNQAMKGRFEELSAWTEKQKEERQLFEiQSKEAKERLKALSHENERLKEELGKLKEK 117
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 118 SERpFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEG 197
Cdd:COG4717 162 EEE-LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 198 EAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQLLLCLRegnqkverLEIALREAKERISDFEKkanghs 277
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL--------FLLLAREKASLGKEAEE------ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 278 AIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQ-----EKCQALERKNSATPSE- 351
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleQEIAALLAEAGVEDEEe 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 352 -------LNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEE--KSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKV 422
Cdd:COG4717 387 lraaleqAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420
....*....|....*....|.
gi 1938958523 423 DKVQLQELSEKLELAEQALAS 443
Cdd:COG4717 467 EDGELAELLQELEELKAELRE 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
79-466 |
4.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 79 QKEERQLFEIQSKEAKERLKALshenERLKEELGKLKEKSERPFEDITGRcgfprtdleQEVEQLKRQVEQEVEHLKNQV 158
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKEL----KELEEELKEAEEKEEEYAELQEEL---------EELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 159 RRLQAEKA--DLLGIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTdsismgKCTEDARTCVEFEEL 236
Cdd:COG4717 119 EKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE------ELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 237 TVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVG---------------- 300
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsli 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 301 ---------------IEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKL 365
Cdd:COG4717 273 ltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 366 ELQVESMRSEIKMEQ-------------AKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSE 432
Cdd:COG4717 353 LREAEELEEELQLEEleqeiaallaeagVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430
....*....|....*....|....*....|....
gi 1938958523 433 KLELAEQALASKQLQMDEMKQTIAKQEEDLETMA 466
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLE 466
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-418 |
4.05e-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: 43.52 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAwtEKQKEERQLFEIQSkeakerlkalshENERLKEELGKLKEK 117
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLK--EKEALERQKEAIER------------QLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 118 serpFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLnssgssEDSFVEIRMTEG 197
Cdd:TIGR02169 260 ----ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL------EDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 198 EAEGAMKEMRNSAGPTRTDSISMGKCTEdartcvEFEELTVSqlllcLREGNQKVERLEIALREAKERISDFEKKAnghs 277
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTE------EYAELKEE-----LEDLRAELEEVDKEFAETRDELKDYREKL---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 278 aietqtegstqkeeedkdpESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALErknsatpSELNEKQE 357
Cdd:TIGR02169 395 -------------------EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE-------EEKEDKAL 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938958523 358 lvysnrklelQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQ 418
Cdd:TIGR02169 449 ----------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
38-336 |
5.38e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEK 117
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 118 SERpfeditgrcgfpRTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEG 197
Cdd:COG1196 308 EER------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 198 EAEGAMKEMRNSAgptrtdsismgkcTEDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHS 277
Cdd:COG1196 376 EAEEELEELAEEL-------------LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1938958523 278 AIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQE 336
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-507 |
7.66e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 34 TFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERqlfeiqskeakERLKALSHENERLKEElgk 113
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-----------EELKKILAEDEKLLDE--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 114 lKEKSERPFEDITGRcgfprtdlEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSgssedsfvEIR 193
Cdd:pfam05483 424 -KKQFEKIAEELKGK--------EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE--------KLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 194 MTEGEAEGAMKEMRNSAGPTRTD--SISMGKCTEDARTCVEFEELTVSQLllclregnQKVERLEIALREAKERISDfek 271
Cdd:pfam05483 487 NIELTAHCDKLLLENKELTQEASdmTLELKKHQEDIINCKKQEERMLKQI--------ENLEEKEMNLRDELESVRE--- 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 272 kanghSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSE 351
Cdd:pfam05483 556 -----EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 352 LNEKQELVysnRKLELQVESMRSEIkmeQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEkVDKVQLQELS 431
Cdd:pfam05483 631 LNAYEIKV---NKLELELASAKQKF---EEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE-IDKRCQHKIA 703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938958523 432 EKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKEN 507
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-484 |
7.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 303 VETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELN-------------EKQELVYSNRKLElQV 369
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaELERLDASSDDLA-AL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 370 ESMRSEIKMEQAKTEEEKSRLATLQATHDkllQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQmd 449
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER-- 765
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1938958523 450 EMKQTIAKQEEDLETMAV-----LRAQMEVYCSDFHAERA 484
Cdd:COG4913 766 ELRENLEERIDALRARLNraeeeLERAMRAFNREWPAETA 805
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
82-461 |
8.35e-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: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 82 ERQLFEIQSK-EAKERLKALSHENERLKEELGKLKEK----------SERPFEDITGRCGFPRTDLE---QEVEQLKRQV 147
Cdd:pfam15921 447 ERQMAAIQGKnESLEKVSSLTAQLESTKEMLRKVVEEltakkmtlesSERTVSDLTASLQEKERAIEatnAEITKLRSRV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 148 E---QEVEHLKNQVRRLQAEKADllgiVSELQLKLnssgSSEDSFVEIRMTEGEAEGAM-KEMRNSAGPTRTDSISMGKC 223
Cdd:pfam15921 527 DlklQELQHLKNEGDHLRNVQTE----CEALKLQM----AEKDKVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 224 TEDARtcVEFEELTVSQlllclregnqkvERLEIALREAKERISDFE----KKANGHS----AIETQTEGSTQKEEEDK- 294
Cdd:pfam15921 599 INDRR--LELQEFKILK------------DKKDAKIRELEARVSDLElekvKLVNAGSerlrAVKDIKQERDQLLNEVKt 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 295 ---DPESVGIEVETLNVQVASLFKELQEAHTKLseaelmKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVES 371
Cdd:pfam15921 665 srnELNSLSEDYEVLKRNFRNKSEEMETTTNKL------KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 372 MRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNK---ALRTIEELTKQQAEKVDKVQLQE--LSEKLELAEQALASKQL 446
Cdd:pfam15921 739 KRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqELSTVATEKNKMAGELEVLRSQErrLKEKVANMEVALDKASL 818
|
410
....*....|....*
gi 1938958523 447 QMDEMKQTIAKQEED 461
Cdd:pfam15921 819 QFAECQDIIQRQEQE 833
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
314-465 |
9.34e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 314 FKELQEAHTklsEAELMKKRLQEKCQAL----ERKN----SATPSELNEKQELVYSNRKLELQVESMRSEIKME----QA 381
Cdd:PRK04863 937 FEQLKQDYQ---QAQQTQRDAKQQAFALtevvQRRAhfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQlrqaQA 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 382 KTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQ---QAEKVDKVQLQELSEKL-------ELAEQALASKQLQMDEM 451
Cdd:PRK04863 1014 QLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsGAEERARARRDELHARLsanrsrrNQLEKQLTFCEAEMDNL 1093
|
170
....*....|....
gi 1938958523 452 KQTIAKQEEDLETM 465
Cdd:PRK04863 1094 TKKLRKLERDYHEM 1107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
287-473 |
1.17e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 287 TQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELV------- 359
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 360 YSN--------------------------RKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEhnkALRTIEE 413
Cdd:COG3883 96 YRSggsvsyldvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE---LEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 414 LTKQQAEKvdKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQME 473
Cdd:COG3883 173 LEAQQAEQ--EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
315-458 |
1.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 315 KELQEAHTKLSEAELMKKRLQEKCQALERKNSATP--------SELNEKQELVY----SNRKLELQVESMRSEIKMEQAK 382
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHtelqSKMRSRAKLLMKRAAHVKQQSS 339
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938958523 383 TEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQ 458
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-416 |
2.35e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 38 EELLQQMKELLVENHQLKEAMklnnQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEK 117
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 118 SERPFEDITG-------------RCGFPRTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGS 184
Cdd:TIGR02168 756 LTELEAEIEEleerleeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 185 SEDSFVEIRMTEGEAEGAMKEMRnsagptrtdsismgkctedartcVEFEELTVSqlllcLREGNQKVERLEIALREAKE 264
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLA-----------------------AEIEELEEL-----IEELESELEALLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 265 RISDFEKkanghsaiETQTEGSTQKEEEDKdpesvgieVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERK 344
Cdd:TIGR02168 888 ALALLRS--------ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 345 NSATPSELNEKQELvySNRKLELQVESMRSEIK---------MEQAktEEEKSRLATLQATHDKLLQEHNKALRTIEELT 415
Cdd:TIGR02168 952 TLEEAEALENKIED--DEEEARRRLKRLENKIKelgpvnlaaIEEY--EELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
.
gi 1938958523 416 K 416
Cdd:TIGR02168 1028 R 1028
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
250-447 |
2.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 250 QKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVAslfkELQEAHTKLSEAEL 329
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELE----RLDASSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 330 MKKRLQEKCQALERknsatpselnEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQAThdkLLQEHNKALR 409
Cdd:COG4913 693 QLEELEAELEELEE----------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA---LLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*...
gi 1938958523 410 tIEELTKQQAEKVDKvQLQELSEKLELAEQALASKQLQ 447
Cdd:COG4913 760 -GDAVERELRENLEE-RIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
245-464 |
3.03e-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: 40.39 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 245 LREGNQKVERLEIALREAKERISDF--EKKANGHSAIETQTEGSTQKEEEDKDPESVGIE-VETLNVQVASLFKELQEah 321
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiISQLNEQISQLKKELTN-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 322 tKLSEAELMKKRLQEKCQALErknsatpSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLL 401
Cdd:TIGR04523 354 -SESENSEKQRELEEKQNEIE-------KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 402 QEH-------NKALRTIEELTKQQAEKvdKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLET 464
Cdd:TIGR04523 426 KEIerlketiIKNNSEIKDLTNQDSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
364-473 |
3.04e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 364 KLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALrtieeltkqQAEKVDKVQLQELSEKLELAEQALAs 443
Cdd:cd22656 132 KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAI---------ARKEIKDLQKELEKLNEEYAAKLKA- 201
|
90 100 110
....*....|....*....|....*....|
gi 1938958523 444 kqlQMDEMKQTIAKQEEDLETMAVLRAQME 473
Cdd:cd22656 202 ---KIDELKALIADDEAKLAAALRLIADLT 228
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
133-460 |
3.64e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 133 RTDLEQEVEQLKRQVEQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMKEMRNSAGP 212
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 213 TRTDSISMGKCTEDArtcvefeeltvsqlllcLREGNQKVERLEIALREAKERIsdfeKKANGhsaietqtegstQKEEE 292
Cdd:pfam07888 123 QRAAHEARIRELEED-----------------IKTLTQRVLERETELERMKERA----KKAGA------------QRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 293 DKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERK----------NSATPSELNEKQE-LVYS 361
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKlttahrkeaeNEALLEELRSLQErLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 362 NRKLELQVESMRSEIKM-EQAKTEEEKSRL----ATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLEL 436
Cdd:pfam07888 250 ERKVEGLGEELSSMAAQrDRTQAELHQARLqaaqLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330 340
....*....|....*....|....
gi 1938958523 437 AEQALASKQLQMDEMKQTIAKQEE 460
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKD 353
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
63-463 |
4.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 63 QAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDIT-GRCGFPRTDLEQEVE 141
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 142 QLKRQVEQEVEHLKNQVRRLQ---AEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEGEAEGAMKEMrnsAGPTRTDSI 218
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL---TGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 219 SMGKCTEDARTCVEFEELTVSQLllcLREGNQKVERLEIALREAKERisdfEKKANGHSAIETQTEGSTQKEEEDKDPES 298
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIEELKKA----KGKCPVCGRELTEEHRKELLEEYTAELKR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 299 VGIEVETLNVQVASLFKELQEAHTKLS-EAELMK-KRLQEKCQALERK-NSATPSELNEKQELVYSNRKLELQVESMRSE 375
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKkESELIKlKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 376 IKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKvQLQELSE------KLELAEQALASKQLQMD 449
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE-RLKELEPfyneylELKDAEKELEREEKELK 622
|
410
....*....|....
gi 1938958523 450 EMKQTIAKQEEDLE 463
Cdd:PRK03918 623 KLEEELDKAFEELA 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
302-472 |
4.46e-03 |
|
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: 39.75 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 302 EVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnRKLELQVESMRSEIKmeqA 381
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---AELEKEIAELRAELE---A 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 382 KTEEEKSRLATLQATHD----KLL------QEHNKALRTIEELTKQQAEKVDkvQLQELSEKLELAEQALASKQLQMDEM 451
Cdd:COG4942 102 QKEELAELLRALYRLGRqpplALLlspedfLDAVRRLQYLKYLAPARREQAE--ELRADLAELAALRAELEAERAELEAL 179
|
170 180
....*....|....*....|.
gi 1938958523 452 KQTIAKQEEDLETMAVLRAQM 472
Cdd:COG4942 180 LAELEEERAALEALKAERQKL 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
316-463 |
4.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 316 ELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnRKLELQVESMRSEIKMEQAKTEEEKSRLATLQA 395
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938958523 396 THD-----KLLQEHNKALRTIEELTKQQAEKVDKVQ--LQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLE 463
Cdd:COG1579 88 NKEyealqKEIESLKRRISDLEDEILELMERIEELEeeLAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
77-420 |
5.61e-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: 39.72 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 77 EKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEkSERPFEDITGRcgfpRTDLEQEVEQLKRQVEQEVEHLKN 156
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEE-AEKARQAEMDR----QAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 157 QVRRLQAEKADLLGIVSELQlklnssgssedsfveiRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEEL 236
Cdd:pfam17380 356 EERKRELERIRQEEIAMEIS----------------RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 237 TVSQLLlclrEGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPEsvgievetlnvqvasLFKE 316
Cdd:pfam17380 420 VEMEQI----RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKK---------------LELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 317 LQEAHTKLSEAE---LMKKRLQEKCQAL---ERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRL 390
Cdd:pfam17380 481 KEKRDRKRAEEQrrkILEKELEERKQAMieeERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|
gi 1938958523 391 ATLQATHDKLLQEHNKALRTIEELTKQQAE 420
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
302-469 |
5.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 302 EVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPsELNEKQELVYSNRKLELQVESMRSEIKmeqa 381
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEELEERLE---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 382 KTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKvQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEED 461
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
....*...
gi 1938958523 462 LETMAVLR 469
Cdd:COG4717 236 LEAAALEE 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
70-486 |
7.75e-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: 39.44 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 70 EELSAWTEKQKEERQLFEIQSKEAKERLKAlshENERLKEELGKLKEKSERPFEDItgrcgfpRTDLEQEVEQLKRQVEQ 149
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVA-------EDDLQALESELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 150 evehlknQVRRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMTEGEAEgAMKEMRNSAGPTRTDSISmgkctEDART 229
Cdd:pfam12128 431 -------GKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE-RAREEQEAANAEVERLQS-----ELRQA 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 230 CVEFEELTVSqlllcLREGNQKVERLEIALREAKERISD--------FEKKANGHSAIETQTEGSTQKEEEDKDPESV-- 299
Cdd:pfam12128 498 RKRRDQASEA-----LRQASRRLEERQSALDELELQLFPqagtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWdg 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 300 ---------GIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQ------ELVYSNRK 364
Cdd:pfam12128 573 svggelnlyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASreetfaRTALKNAR 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 365 LELQ---VESMRSEIKMEQAKTEEEKS---RLATLQATHDKLLQEHNKALRTIEE------LTKQQAEKV----DKVQLQ 428
Cdd:pfam12128 653 LDLRrlfDEKQSEKDKKNKALAERKDSaneRLNSLEAQLKQLDKKHQAWLEEQKEqkrearTEKQAYWQVvegaLDAQLA 732
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1938958523 429 ELSEKLELAEQALASKQLQMDE-MKQTIAKQEEDLETMAVLRAQMEvycsDFHA--ERAAR 486
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALETwYKRDLASLGVDPDVIAKLKREIR----TLERkiERIAV 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
78-463 |
8.04e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 78 KQKEERQLFEIQskEAKERLKALSHENERLKEELGKLKEKSERpFEDITGR--------CGFPRTDLEQEVEQLKRQV-- 147
Cdd:TIGR02168 174 RKETERKLERTR--ENLDRLEDILNELERQLKSLERQAEKAER-YKELKAElrelelalLVLRLEELREELEELQEELke 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 148 -EQEVEHLKNQVRRLQAEKADLLGIVSELQLKLNssgssedsfveirmtegEAEGAMKEMrnsagptrtdsismgkcted 226
Cdd:TIGR02168 251 aEEELEELTAELQELEEKLEELRLEVSELEEEIE-----------------ELQKELYAL-------------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 227 artcvefeeltvsqlllclregNQKVERLEIALREAKERISDFEKKAnghSAIETQTEGSTQKEEEDK-DPESVGIEVET 305
Cdd:TIGR02168 294 ----------------------ANEISRLEQQKQILRERLANLERQL---EELEAQLEELESKLDELAeELAELEEKLEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 306 LNVQVASLFKELQEAHTKLSEaelMKKRLQEKCQALERKNsatpSELNEKQELVYSNRKlelQVESMRSEIKMEQAKTEE 385
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEE---LESRLEELEEQLETLR----SKVAQLELQIASLNN---EIERLEARLERLEDRRER 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938958523 386 EKSRLATL-QATHDKLLQEHNKALRTIEELTKQQAEKVDKV--QLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDL 462
Cdd:TIGR02168 419 LQQEIEELlKKLEEAELKELQAELEELEEELEELQEELERLeeALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
.
gi 1938958523 463 E 463
Cdd:TIGR02168 499 E 499
|
|
| |
