|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
242-509 |
7.36e-111 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 333.59 E-value: 7.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 242 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 312
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 313 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSE 392
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 393 IATNGEtsdTLNNVGYQGPTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSE 470
Cdd:pfam09738 190 ENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPD 266
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622852882 471 DDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 509
Cdd:pfam09738 267 GFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-583 |
1.30e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 270 GGTSSRRGSGDTsisidteasiREIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEE 349
Cdd:TIGR02169 658 GSRAPRGGILFS----------RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 350 KNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVgyqgptkmtKAELNALKstgDGT 429
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL---------EEALNDLE---ARL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 430 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITA 509
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQ--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852882 510 LEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 583
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-583 |
2.94e-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: 56.99 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 264 ATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 343
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 344 RRQYEEKNKEFER-----EKHAHSILQFQFaEVKEALKEREEMLEKHGIiLNSEIATNGETSDTLnnvgyQGPTKMTKAE 418
Cdd:TIGR02168 725 SRQISALRKDLARleaevEQLEERIAQLSK-ELTELEAEIEELEERLEE-AEEELAEAEAEIEEL-----EAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 419 LNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKldnlRSEDDVLEngtdmhvmdlqrdANRQ 492
Cdd:TIGR02168 798 LKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----ELSEDIES-------------LAAE 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 493 ISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEK 572
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEG 933
|
330
....*....|.
gi 1622852882 573 MKANRSALLSQ 583
Cdd:TIGR02168 934 LEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-559 |
1.69e-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: 51.21 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 286 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLkdmlleleeqlaesRRQYEEKNKEFEREKhahsILQ 365
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL--------------REALDELRAELTLLN----EEA 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 366 FQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNnvgyqgptkmtkAELNALKSTGDgTLDIRLKKLVDERECLL 445
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA------------AEIEELEELIE-ELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 446 EQIKKLKGQLEERQKigKLDNLRSEddvlengtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RY 524
Cdd:TIGR02168 887 EALALLRSELEELSE--ELRELESK---------------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEY 949
|
250 260 270
....*....|....*....|....*....|....*
gi 1622852882 525 KSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 559
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
429-583 |
3.05e-06 |
|
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: 48.77 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 429 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 495
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 496 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEelevsnghlvKRLEKMKA 575
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE----------AELEELEA 163
|
....*...
gi 1622852882 576 NRSALLSQ 583
Cdd:COG1579 164 EREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
433-584 |
4.80e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 433 RLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTdmhvmdlqRDANRQISDLKFKLAKSEQEITALEQ 512
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEE--ELEQARSELEQLEEEL--------EELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852882 513 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 584
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
281-583 |
5.11e-06 |
|
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: 49.73 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 281 TSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TNFMYQVDTLKDMLLELEEQL 340
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRNVQTECEALKLQMAEKDKVI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 341 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSdtlnnvgyqgpTKMTKAELN 420
Cdd:pfam15921 565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE-----------ARVSDLELE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 421 ALKSTGDGTLDIR-LKKLVDERECLLEQIKKLKGQL----EERQKIGKldNLRSEDDVLENGTD---MHVMDLQRDANRQ 492
Cdd:pfam15921 634 KVKLVNAGSERLRaVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKR--NFRNKSEEMETTTNklkMQLKSAQSELEQT 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 493 ISDLK---------FKLAKSEQ-EITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---E 558
Cdd:pfam15921 712 RNTLKsmegsdghaMKVAMGMQkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagE 791
|
330 340
....*....|....*....|....*
gi 1622852882 559 LEVSNGHlVKRLEKMKANRSALLSQ 583
Cdd:pfam15921 792 LEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-584 |
1.79e-05 |
|
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: 47.71 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 430 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK 499
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 500 ---LAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLV 567
Cdd:TIGR04523 488 qkeLKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKN 567
|
170
....*....|....*..
gi 1622852882 568 KRLEKMKANRSALLSQQ 584
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQ 584
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
289-577 |
2.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 289 ASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTN---FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQ 365
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 366 FQFAEVKEALKEREEmLEKHGIILNSEIAT----NGETSDTLNNVGYqGPTKMTKAELNALKSTGDGTldIRLKKLVDER 441
Cdd:PRK03918 539 GEIKSLKKELEKLEE-LKKKLAELEKKLDEleeeLAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 442 ECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQV 521
Cdd:PRK03918 615 EREEKELKKLEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSREL 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852882 522 SRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 577
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-560 |
5.66e-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: 46.21 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 286 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLleleeqlaeSRRQYEEKNKEFEREKHAHSILQ 365
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL---------SHSRIPEIQAELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 366 FQFAEVKEALKEREEMLEkhgiILNSEIATNGETSDTLNNvgyqgPTKMTKAELNALKsTGDGTLDIRLKKLVDERECLL 445
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKE----YLEKEIQELQEQRIDLKE-----QIKSIEKEIENLN-GKKEELEEELEELEAALRDLE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 446 EQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYK 525
Cdd:TIGR02169 882 SRLGDLKKERDELEA--QLRELERKIEELEAQIE--------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852882 526 SA---AENAEKIE------------------------DELKAEKRKLQRELRSALDKTEELE 560
Cdd:TIGR02169 952 SLedvQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
433-584 |
6.61e-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: 46.20 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 433 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 501
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 502 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 581
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 1622852882 582 SQQ 584
Cdd:TIGR02168 393 LQI 395
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
344-580 |
9.14e-05 |
|
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: 45.14 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 344 RRQYEEKNKEFEREKhahsilqfqfAEVKEALKEREEmlekhgiiLNSEIAtngETSDTLNNvgyqgptkmTKAELNALK 423
Cdd:COG4942 33 QQEIAELEKELAALK----------KEEKALLKQLAA--------LERRIA---ALARRIRA---------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 424 StgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhvmdlqRDANRQISDLKFK 499
Cdd:COG4942 83 A--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF------LDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 500 LAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSA 579
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
.
gi 1622852882 580 L 580
Cdd:COG4942 225 L 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
314-575 |
9.59e-05 |
|
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: 45.49 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 314 QLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREkhahsiLQFQFAEVKEALKEREEMLEKHGIILNS-- 391
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESGNLDDQlq 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 392 -----------EIATNGETS------DTLNNVGYQG----------PTKMTKAELNALKSTGDGTLDIRLKKLVDERECl 444
Cdd:pfam15921 381 klladlhkrekELSLEKEQNkrlwdrDTGNSITIDHlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNES- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 445 LEQIKKLKGQLEERQKIGK--LDNLRSEDDVLENgtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQV- 521
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRkvVEELTAKKMTLES------------SERTVSDLTASLQEKERAIEATNAEITKLRSRVd 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852882 522 ------SRYKSAAENAEKIEDELKA------EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 575
Cdd:pfam15921 528 lklqelQHLKNEGDHLRNVQTECEAlklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-564 |
1.11e-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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 286 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLkdmlleleeqlaesRRQYEEKNKEfeREKhahsilq 365
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL--------------EREIEEERKR--RDK------- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 366 fqfaeVKEALKEREEMLEKHGIILNSEIATNGETSDTLnnVGYQGPTKMTKAELNALKSTGDgtldirlkKLVDERECLL 445
Cdd:TIGR02169 355 -----LTEEYAELKEELEDLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELD--------RLQEELQRLS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 446 EQIKKLKGQLEerqkigkldnlRSEDDVLENGTDMHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRy 524
Cdd:TIGR02169 420 EELADLNAAIA-----------GIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK- 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622852882 525 ksaaenAEKIEDELKAEKRKLQRELRSALDKTEELEVSNG 564
Cdd:TIGR02169 488 ------LQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
344-553 |
1.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 344 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEiatngetsdtlnnvgyqgptkmtkaelnalk 423
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------------------------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 424 stgdgTLDIRLKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 502
Cdd:COG4717 129 -----PLYQELEALEAELAELPERLEELEERLEElRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622852882 503 SEQEITALEQNVIRLESQVSRYKSAAENAEKiEDELKAEKRKLQRELRSAL 553
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-584 |
2.44e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 345 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemLEKHGIILNSEIATNGETSDTLNNvgyqgptkmTKAELNALks 424
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEE---------LRLELEEL-- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 425 tgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIG-KLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKS 503
Cdd:COG1196 280 --ELELEEAQAEEYELLAELARLEQDIARLEERRRELEeRLEELEEELAELE--------EELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 504 EQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 583
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 1622852882 584 Q 584
Cdd:COG1196 430 L 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-580 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 370 EVKEALKEREEMLEKHGIilnSEIATNGETSDTLNN--VGYQGPTKMTKAELNALKStgdgtLDIRLKKLVDERECLLEQ 447
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNL---EELEKKAEEYEKLKEklIKLKGEIKSLKKELEKLEE-----LKKKLAELEKKLDELEEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 448 IKKLKGQLEERqKIGKLDNLRSEDDVLENGTDMHVMdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA 527
Cdd:PRK03918 572 LAELLKELEEL-GFESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852882 528 AENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 580
Cdd:PRK03918 649 LEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
433-575 |
3.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 433 RLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLE-----NGTDmHVMDLQRD-----------------AN 490
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEA--RLDALREELDELEaqirgNGGD-RLEQLEREierlereleererrrarLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 491 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 570
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*
gi 1622852882 571 EKMKA 575
Cdd:COG4913 443 LALRD 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
344-584 |
5.14e-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: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 344 RRQYEEKNKEFEREKHAHSILQFQFAEVKEA---LKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtKAELN 420
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEEL------------EEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 421 ALKSTGDG------TLDIRLKKLVDERECLLEQIKKLKGQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQIS 494
Cdd:COG1196 327 ELEEELEEleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 495 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 574
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|
gi 1622852882 575 ANRSALLSQQ 584
Cdd:COG1196 484 EELAEAAARL 493
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
525-584 |
6.31e-04 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.83 E-value: 6.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 525 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 584
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
439-580 |
8.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 439 DERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENgtdmHVMDLQRDANR-----QISDLKFKLAKSEQEITALEQ 512
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyAELQEELEELEEELEELEA----ELEELREELEKlekllQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852882 513 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSnghLVKRLEKMKANRSAL 580
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAEL 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
293-550 |
8.19e-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: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 293 EIKDSLAEVEEKYK-KAMVSNAQLDNEKTN---FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 368
Cdd:pfam05483 545 NLRDELESVREEFIqKGDEVKCKLDKSEENarsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 369 AEVKEALKEREEMLEKHGIILNSEIATNGETSDTlnnvgYQGptkmtkaelnalkstgdgtlDIRLKKLVDERecLLEQI 448
Cdd:pfam05483 625 SAENKQLNAYEIKVNKLELELASAKQKFEEIIDN-----YQK--------------------EIEDKKISEEK--LLEEV 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 449 KKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKS-EQEITALEqnvIRLESQVSRYKSA 527
Cdd:pfam05483 678 EKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNkEQEQSSAK---AALEIELSNIKAE 754
|
250 260
....*....|....*....|...
gi 1622852882 528 AENAEKIEDELKAEKRKLQRELR 550
Cdd:pfam05483 755 LLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
353-541 |
8.39e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 353 EFEREKHAHSILQFQfAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVGYQ--------GPTKMTKAELNALKS 424
Cdd:TIGR00618 735 AAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlreedtHLLKTLEAEIGQEIP 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 425 TGDGTLDIRLKKLVDERECLLEQIKKL-KGQLEERQKIGKL-DNLRSEDDVLENGTDMHVMDLQRDANRQISDLK--FKL 500
Cdd:TIGR00618 814 SDEDILNLQCETLVQEEEQFLSRLEEKsATLGEITHQLLKYeECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFdgDAL 893
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622852882 501 AKSEQEITAleQNVIRLESQ-----VSRY--KSAAENAEKIEDELKAE 541
Cdd:TIGR00618 894 IKFLHEITL--YANVRLANQsegrfHGRYadSHVNARKYQGLALLVAD 939
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
449-578 |
8.82e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.55 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 449 KKLKGQLEERQKI-GKLDNLRSEDDVLENGTDMHVMDLQ---RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-- 522
Cdd:pfam04849 171 EKLRGLEEENLKLrSEASHLKTETDTYEEKEQQLMSDCVeqlSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVdl 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852882 523 --RYKSAAENAEKIEDELKAEK---RKLQRELRSALDKTEELEvsnGHLVKRLEKMKANRS 578
Cdd:pfam04849 251 qhKCKELGIENEELQQHLQASKeaqRQLTSELQELQDRYAECL---GMLHEAQEELKELRK 308
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-584 |
9.91e-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: 42.35 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 329 LKDMLLELEEQLAESRRQ------YEEKNKEFEREKHAHSILQFQFA-----EVKEALKEREEMLEKhgiiLNSEIATng 397
Cdd:TIGR02168 191 LEDILNELERQLKSLERQaekaerYKELKAELRELELALLVLRLEELreeleELQEELKEAEEELEE----LTAELQE-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 398 etsdtlnnvgyqgptkmTKAELNALKStGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENg 477
Cdd:TIGR02168 265 -----------------LEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRE--RLANLERQLEELEA- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 478 tdmhvmDLQRDANRQIsDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALdktE 557
Cdd:TIGR02168 324 ------QLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---L 393
|
250 260 270
....*....|....*....|....*....|
gi 1622852882 558 ELEVSNGHLV---KRLEKMKANRSALLSQQ 584
Cdd:TIGR02168 394 QIASLNNEIErleARLERLEDRRERLQQEI 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-575 |
1.10e-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: 41.97 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 289 ASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDmlleleeQLAESRRQYEEKNKEFerekHAHSILQFQF 368
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEELQKEL----YALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 369 AEVKEALKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtKAELNALKstgdgtldirlkklvderecllEQI 448
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDEL------------AEELAELE----------------------EKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 449 KKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAA 528
Cdd:TIGR02168 347 EELKEELESLEA--ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622852882 529 ENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 575
Cdd:TIGR02168 417 ERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
489-581 |
1.58e-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: 40.90 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 489 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 568
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|...
gi 1622852882 569 RLEKMKANRSALL 581
Cdd:COG4942 98 ELEAQKEELAELL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
444-580 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 444 LLEQIKKLKG---QLEE-RQKIGKLDNLRseddvlENGTDMHVMDLQRDANRQIsDLKFKLAKSEQEITALEQNVIRLES 519
Cdd:COG4913 230 LVEHFDDLERaheALEDaREQIELLEPIR------ELAERYAAARERLAELEYL-RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852882 520 QVSRYKSAAENAEKIEDELKAEKRKLQRELRSA-LDKTEELEVSNGHLVKRLEKMKANRSAL 580
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARL 364
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
429-575 |
2.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 429 TLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLEngtdmHVMDLQRDANRQISDLKFKLAKSEQEIT 508
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-----ERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852882 509 ALEQNVIRLESQVS-----RYKSAAENAEKIED---ELKAEKRKLQRELRSALDKTEELEVS--NGHLVKRLEKMKA 575
Cdd:COG4717 174 ELQEELEELLEQLSlateeELQDLAEELEELQQrlaELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARL 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-531 |
2.26e-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: 40.52 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 289 ASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 368
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 369 AEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDERECLLE 446
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 447 QIKKLKGQLEERQKigKLDNLRSEDDvlengtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKS 526
Cdd:COG4942 175 ELEALLAELEEERA--ALEALKAERQ-----------KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 1622852882 527 AAENA 531
Cdd:COG4942 242 RTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-576 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 341 AESRRQYEEKNKEFEREKH---AHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtKA 417
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL------------AE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 418 ELNAL--KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLENGTDMHVMDLQRdANRQISD 495
Cdd:TIGR02168 338 ELAELeeKLEELKEELESLEAELEELEAELEELESRLEELEE-----QLETLRSKVAQLELQIASLNNEIER-LEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 496 LKFKLAKSEQEITAL-----EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQ---RELRSALDKTEELEVSNGHLV 567
Cdd:TIGR02168 412 LEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELReelEEAEQALDAAERELAQLQARL 491
|
....*....
gi 1622852882 568 KRLEKMKAN 576
Cdd:TIGR02168 492 DSLERLQEN 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-533 |
2.36e-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: 40.52 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 286 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFERekhahsiLQ 365
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-------LR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 366 FQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDEREC 443
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 444 LLEQIKKLKGQLEERQKigKLDNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSR 523
Cdd:COG4942 172 ERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|
gi 1622852882 524 YKSAAENAEK 533
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
440-572 |
2.91e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 440 ERECLLEQIKKLKGQLEErqkigkldnLRSEDDVLENgtDMHVMDlqrdanRQISDLKFKL----------AKSEQEITA 509
Cdd:COG2433 407 ELTEEEEEIRRLEEQVER---------LEAEVEELEA--ELEEKD------ERIERLERELsearseerreIRKDREISR 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852882 510 LEQNVIRLESQVsryksaaenaekieDELKAEKRKLQRELRSaLDKTEELEVSNGHL-VKRLEK 572
Cdd:COG2433 470 LDREIERLEREL--------------EEERERIEELKRKLER-LKELWKLEHSGELVpVKVVEK 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
431-561 |
3.24e-03 |
|
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: 40.44 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 431 DIRLKKLVDERECLLEQIKKLKGQLEERQK-IGKLDNLRSE--------DDVLENGTDmHVMDL----QRDANRQISDLK 497
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEeLEKLTEEISElekrleeiEQLLEELNK-KIKDLgeeeQLRVKEKIGELE 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852882 498 FKLAKSEQEITALEQNVIRLE-------SQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEV 561
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEerlakleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
415-564 |
4.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 415 TKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEERQK---------------IGKLDNL---RSEDDVLEN 476
Cdd:COG3883 49 LNEEYNELQA--------ELEALQAEIDKLQAEIAEAEAEIEERREelgeraralyrsggsVSYLDVLlgsESFSDFLDR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 477 --------GTDMHVMDLQRDANRQISDLKFKLAKSEQEITA----LEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRK 544
Cdd:COG3883 121 lsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEAlkaeLEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
170 180
....*....|....*....|
gi 1622852882 545 LQRELRSALDKTEELEVSNG 564
Cdd:COG3883 201 LEAELAAAEAAAAAAAAAAA 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
491-572 |
5.42e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 491 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 570
Cdd:PRK12704 68 KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
..
gi 1622852882 571 EK 572
Cdd:PRK12704 145 ER 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
405-584 |
5.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 405 NVGYQGPT-KMTKAELNAL-KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDV--LENGTDM 480
Cdd:COG3206 139 EISYTSPDpELAAAVANALaEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEA--ALEEFRQKNGLvdLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 481 HVMDLQrDANRQISDLKFKLAKSEQEITALEQNV---------------------------IRLESQVSRYKSAAENAEK 533
Cdd:COG3206 217 LLQQLS-ELESQLAEARAELAEAEARLAALRAQLgsgpdalpellqspviqqlraqlaeleAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622852882 534 IEDELKAEKRKLQRELRSALDKTE----ELEVSNGHLVKRLEKMKANRSALLSQQ 584
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEaeleALQAREASLQAQLAQLEARLAELPELE 350
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
429-549 |
6.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 429 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK----IGKLDNLRSEDDVLEnGTDMHVMDLQRD-------------ANR 491
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQErreaLQRLAEYSWDEIDVA-SAEREIAELEAElerldassddlaaLEE 692
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852882 492 QISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQREL 549
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
346-572 |
8.06e-03 |
|
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: 39.32 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 346 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKhgiilNSEIATNGETsdtlnnvgyqgpTKMTKAELNALKST 425
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-----KKQFEKIAEE------------LKGKEQELIFLLQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 426 GDGT---LDIRLKKLVDERECLLEQIKKLKGQLEERqkigKLDNLRseddvLENGTDMHVMDlQRDANRQISDLKFKLAK 502
Cdd:pfam05483 448 REKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKE----KLKNIE-----LTAHCDKLLLE-NKELTQEASDMTLELKK 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622852882 503 SEQEITALEQNVIRLESQVsryKSAAENAEKIEDELKAEKRKLQR---ELRSALDKTEELEVSNGHLVKRLEK 572
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQI---ENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
267-552 |
8.23e-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: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 267 ASLGGTSSRRGSGDTSISiDTEASIREIKDSLAEVEEKYKKAmvsNAQLdnEKTNfmyqvdtlkdmlleleeqlaesrRQ 346
Cdd:COG3883 2 LALALAAPTPAFADPQIQ-AKQKELSELQAELEAAQAELDAL---QAEL--EELN-----------------------EE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 347 YEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkaeLNAlKSTG 426
Cdd:COG3883 53 YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852882 427 D--GTLDIrLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSE 504
Cdd:COG3883 116 DflDRLSA-LSKIADADADLLEELKADKAELEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQE 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622852882 505 QEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSA 552
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| |
