|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
141-456 |
2.95e-144 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 417.40 E-value: 2.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 141 QEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGqnlGVTRNNLEPLFEAYLGSMRSTLDRLQSERGRLDSEL 220
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 221 RNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAYMGRMDLHGKVGTLTQEIDFLQQLYEMELSQVQTHVSNTNVV 300
Cdd:pfam00038 78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 301 LSMDNNRNLDLDSIIAEVKAQYELIAQRSRAEAEAWYQTKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAK 380
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32567786 381 KQCQQLQTAIAEAEQRGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESEESR 456
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
30-138 |
8.49e-40 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 141.72 E-value: 8.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 30 RTSFSSVTVSRSSGSGGGAhCGPGTGGFGSRSLYNLGGHKSISVSVAGGAllGRALGGF--------------------- 88
Cdd:pfam16208 14 RRSYSSVSSSRRGGGGGGG-GGGGGGGFGSRSLYNLGGSKSISISVAGGG--SRPGSGFgfgggggggfgggfggggggg 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32567786 89 ---------GFGSRAFMGQGAGRQTFG-------PACPPGGIQEVTVNQSLLTPLHVEIDPEIQRV 138
Cdd:pfam16208 91 fgggggfggGFGGGGYGGGGFGGGGFGgrggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
85-438 |
1.87e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 85 LGGFGFGSRAFMGQGAGRQTFGPACPPGGIQEVTVNQSLLTPLHVEIDPEIQRVRTQERE---QIKTLNNKFASFIDKVR 161
Cdd:TIGR02168 650 LDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 162 FLEQQNKVLETKWALLQEQGQNLGVTRNNLEplfeAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKH 241
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELE----AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 242 TAAENEFVVLKKDVDAAYMGRMDLHGKVGTLTQEIDFLQQlyemELSQVQTHVSNTNVVLsmdNNRNLDLDSIIAEVKAQ 321
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE----QIEELSEDIESLAAEI---EELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 322 YELIAQRSRAEAEAwyQTKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEaeqRGELAL 401
Cdd:TIGR02168 879 LNERASLEEALALL--RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---EYSLTL 953
|
330 340 350
....*....|....*....|....*....|....*..
gi 32567786 402 KDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLA 438
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-390 |
7.89e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 145 QIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGQNLGVTRNNLEplfeaylgsmrSTLDRLQSERGRLDSELRNVQ 224
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN-----------SEIKDLTNQDSVKELIIKNLD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 225 DLVEDFKNK---YEDEIN--KHTAAEN--EFVVLKKDVDAAYMGRMDLHGKVGTLTQEIDFL---QQLYEMELSQVQTHV 294
Cdd:TIGR04523 461 NTRESLETQlkvLSRSINkiKQNLEQKqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLkekIEKLESEKKEKESKI 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 295 SNTNV-VLSMDNNRNldldsiiaevKAQYELIAQRSRAEAEAWYQT------KYEELQVTAGKHGDNLRDTKNEIAELTR 367
Cdd:TIGR04523 541 SDLEDeLNKDDFELK----------KENLEKEIDEKNKEIEELKQTqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
250 260
....*....|....*....|...
gi 32567786 368 TIQRLQGEADAAKKQCQQLQTAI 390
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSII 633
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
310-412 |
1.65e-06 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 47.25 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 310 DLDSIIAEVKAQYELIAQRSRAEAEAW--YQTKYE-ELQvtagKHGD---NLRDTKNEIAELTRTIQRLQGEADAAKKQC 383
Cdd:pfam07926 12 RLKEEAADAEAQLQKLQEDLEKQAEIAreAQQNYErELV----LHAEdikALQALREELNELKAEIAELKAEAESAKAEL 87
|
90 100
....*....|....*....|....*....
gi 32567786 384 QQLQTAIAEAEQRGELALKDAQKKLGDLD 412
Cdd:pfam07926 88 EESEESWEEQKKELEKELSELEKRIEDLN 116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
310-453 |
4.35e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 310 DLDSIIAEVKAQYELIAQRsRAEAEAwyqtKYEELQVTAGKH-GDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQL-- 386
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALRE----ELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALgl 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32567786 387 ------------QTAIAEAEQRGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESE 453
Cdd:COG4913 374 plpasaeefaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-456 |
4.93e-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: 49.67 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 161 RFLEQQNKVLETKWALLqeqGQNLGVTRNNLEPLfeaylgsmRSTLDRLQSERGRLDSELRNVQDLVEDFKNKyedeink 240
Cdd:TIGR02168 214 RYKELKAELRELELALL---VLRLEELREELEEL--------QEELKEAEEELEELTAELQELEEKLEELRLE------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 241 HTAAENEFVVLKKDVDAAYmgrmdlhGKVGTLTQEIDFLQQlyemELSQVQTHVSNTNVVLSMDNNRNLDLDSIIAEVKA 320
Cdd:TIGR02168 276 VSELEEEIEELQKELYALA-------NEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 321 QYELIAQRSRAEAEAW--YQTKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRG- 397
Cdd:TIGR02168 345 KLEELKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIe 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32567786 398 -------ELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESEESR 456
Cdd:TIGR02168 425 ellkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-432 |
5.45e-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: 49.30 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 133 PEIQRVRtqerEQIKTLNNKFASFIDKVRflEQQNKVLETKwALLQEQGQNLGVTRNNLEPLfEAYLGSMRSTLDRLQSE 212
Cdd:TIGR02169 674 AELQRLR----ERLEGLKRELSSLQSELR--RIENRLDELS-QELSDASRKIGEIEKEIEQL-EQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 213 RGRLDSELRNVQDLVEDFKNK---YEDEINKHTAAENEfvvlkkdvdaayMGRMDLHGKVGTLTQEIDFLqqlyEMELSQ 289
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARieeLEEDLHKLEEALND------------LEARLSHSRIPEIQAELSKL----EEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 290 VQTHVSNTNVVLSMDNNRNLDLDSIIAEVKAQYELIAQR--SRAEAEAWYQTKYEELQVTAGKHGDNLRDTKNEIAELTR 367
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32567786 368 TIQRLQGEADAAKKQCQQLQTAIAEAEQRgelalkdaqkkLGDLDVALHQAKEDLTRLLRDYQEL 432
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKR-----------LSELKAKLEALEEELSEIEDPKGED 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-455 |
6.15e-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: 49.30 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 196 EAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAYMGRMDLHGKVGTLTQE 275
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 276 I----DFLQQL------YEMELSQVQTHVSNTNVVLSMDNNRNLD-----LDSIIAEVKAQYELIAQR--SRAEAEAWYQ 338
Cdd:TIGR02169 753 IenvkSELKELearieeLEEDLHKLEEALNDLEARLSHSRIPEIQaelskLEEEVSRIEARLREIEQKlnRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 339 TKYEELQvtagkhgDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAE-QRGELA--LKDAQKKLGDLDVAL 415
Cdd:TIGR02169 833 KEIQELQ-------EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsRLGDLKkeRDELEAQLRELERKI 905
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 32567786 416 HQAKEDLTRlLRDYQELMNVKL-ALDVEIATYRKLLESEES 455
Cdd:TIGR02169 906 EELEAQIEK-KRKRLSELKAKLeALEEELSEIEDPKGEDEE 945
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
310-457 |
2.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 310 DLDSIIAEVKAQYELIAQRSRA----EAEAWYQTKYEELQVTAGKHGD---NLRDTKNEIAELTRTIQRLQGEADAAKKQ 382
Cdd:COG4913 628 EAEERLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAeleRLDASSDDLAALEEQLEELEAELEELEEE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 383 CQQLQTAIAEAEQRgelaLKDAQKKLGDLDVALHQA-----KEDLTRLLRDYQELM------NVKLALDVEIATYRKLLE 451
Cdd:COG4913 708 LDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarLELRALLEERFAAALgdaverELRENLEERIDALRARLN 783
|
....*.
gi 32567786 452 SEESRM 457
Cdd:COG4913 784 RAEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-452 |
5.27e-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: 45.53 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 194 LFEAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAYMGRMDLHGKVGTLT 273
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 274 QEIDFLQQlyemELSQVQTHVSNTNVVLSMDNNRNldldsiiaevkaQYELIAQRSRAEAEAWYQTKYEELqvtagkhgd 353
Cdd:COG4942 90 KEIAELRA----ELEAQKEELAELLRALYRLGRQP------------PLALLLSPEDFLDAVRRLQYLKYL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 354 nLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAE-AEQRGEL--ALKDAQKKLGDLDVALHQAKEDLTRLLRDYQ 430
Cdd:COG4942 145 -APARREQAEELRADLAELAALRAELEAERAELEALLAElEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250 260
....*....|....*....|..
gi 32567786 431 ELMNVKLALDVEIATYRKLLES 452
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
315-458 |
1.01e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 315 IAEVKAQYELIAQRSRAEAEAWYQTKYEELQVTAGK--HGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAE 392
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32567786 393 AEQR---GELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESEESRMS 458
Cdd:COG1196 349 AEEEleeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-460 |
1.02e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 358 TKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQrgelALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKL 437
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100
....*....|....*....|...
gi 32567786 438 ALDVEIATYRKLLESEESRMSGE 460
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEA 773
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-452 |
1.60e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 198 YLG-SMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAYmgrmdLHGKVGTLTQEI 276
Cdd:COG4913 603 VLGfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 277 dflqqlyemelsqvqthvsntnvvlsmdnnRNLDLDSiiAEVKAQYELIAQRSRAEAEAwyQTKYEELQVTAGKHgdnlr 356
Cdd:COG4913 678 ------------------------------ERLDASS--DDLAALEEQLEELEAELEEL--EEELDELKGEIGRL----- 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 357 dtKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEA-------EQRGELALKDAQKKLGDLDVALHQAKEDLTRLLRDY 429
Cdd:COG4913 719 --EKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgDAVERELRENLEERIDALRARLNRAEEELERAMRAF 796
|
250 260
....*....|....*....|....*..
gi 32567786 430 QEL-MNVKLALDVEIAT---YRKLLES 452
Cdd:COG4913 797 NREwPAETADLDADLESlpeYLALLDR 823
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
134-434 |
2.50e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 134 EIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWAL---LQEQGQNLgvtrnnleplfEAylgsmRSTLDRLQ 210
Cdd:pfam06160 122 EVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQfeeLTESGDYL-----------EA-----REVLEKLE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 211 SERGRLDSELRNVQDLVEDFKNKYEDEINK----------------HTAAENEFVVLKKDVDAAY--MGRMDL---HGKV 269
Cdd:pfam06160 186 EETDALEELMEDIPPLYEELKTELPDQLEElkegyremeeegyaleHLNVDKEIQQLEEQLEENLalLENLELdeaEEAL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 270 GTLTQEIDFLQQLYEMELS---QVQTHVSNTNVVLS--MDNNRNL----------------------DLDSIIAEVKAQY 322
Cdd:pfam06160 266 EEIEERIDQLYDLLEKEVDakkYVEKNLPEIEDYLEhaEEQNKELkeelervqqsytlnenelervrGLEKQLEELEKRY 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 323 ELIAQRSrAEAEAWY---QTKYEELQvtagkhgDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGE- 398
Cdd:pfam06160 346 DEIVERL-EEKEVAYselQEELEEIL-------EQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEk 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 32567786 399 -----------LALKDAQKKLGDLDVALHQAK---EDLTRLLRDYQELMN 434
Cdd:pfam06160 418 snlpglpesylDYFFDVSDEIEDLADELNEVPlnmDEVNRLLDEAQDDVD 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-446 |
2.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 134 EIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGQNLGVTRNNLEplfeaylgsmrSTLDRLQSER 213
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-----------EELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 214 GRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAymgrmdlhgkvgtLTQEIDFLQQLYEmELSQVQTH 293
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-------------EEELEELAEELLE-ALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 294 VSNTNVVLSMDNNRNLDLDSIIAEVKAQYELIAQRSRAEAEAwyQTKYEELQvtagkhgDNLRDTKNEIAELTRTIQRLQ 373
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE--EEALEEAA-------EEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32567786 374 GEADAAKKQCQQLQTAIAEAEQRGELALKDAQKKLGDL-DVALHQAKEDLTRLLRDYQELMNVKLALDVEIATY 446
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLeGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
196-447 |
3.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 196 EAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKnkyedeinkhtaAENEFVVLKKDVDAAYMGRMDLHGKVGTLTQE 275
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 276 IDFLQQLYEmelsQVQTHVSNTNVVLSMDNNrnldlDSIIAEVKAQYELiAQRSRAEAEAWYQTKYEELQVTAGKhgdnL 355
Cdd:COG3206 235 LAEAEARLA----ALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-LEAELAELSARYTPNHPDVIALRAQ----I 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 356 RDTKNEI-AELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGeLALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELmn 434
Cdd:COG3206 301 AALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA-- 377
|
250
....*....|...
gi 32567786 435 vKLALDVEIATYR 447
Cdd:COG3206 378 -RLAEALTVGNVR 389
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-458 |
3.76e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 317 EVKAQYELIAQRSRAEAEAWYQTKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQ- 395
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQd 303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32567786 396 --RGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLESEESRMS 458
Cdd:COG1196 304 iaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
130-448 |
4.06e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 130 EIDPEIQRVRTQER-----EQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGQNLGVTRNNLEPLF-------EA 197
Cdd:COG4717 113 ELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslatEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 198 YLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENE---------------FVVLKKDVDAAYMGR 262
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 263 MDLHG---------------------KVGTLTQEIDFLQQLYEMELSQVQTHVSNTNVVLSMDNNRNLDLDSIIAEVKAQ 321
Cdd:COG4717 273 LTIAGvlflvlgllallflllarekaSLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 322 Y----ELIAQRSRAEAEAWYQTKYEELQVT-------AGKHGDNLRDTKNEIAELTR----------------------- 367
Cdd:COG4717 353 LreaeELEEELQLEELEQEIAALLAEAGVEdeeelraALEQAEEYQELKEELEELEEqleellgeleellealdeeelee 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 368 TIQRLQGEADAAKKQCQQLQTAIAEAEQRGELALKDaqKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYR 447
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
.
gi 32567786 448 K 448
Cdd:COG4717 511 E 511
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
195-444 |
4.23e-04 |
|
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: 43.29 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 195 FEAYLGSMRSTLDRLQSERGRLDSELRNVQDLVED----FKNKYEDEINKHTAAENEFVVLKKDVDAAymgrmdlHGKVG 270
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFartaLKNARLDLRRLFDEKQSEKDKKNKALAER-------KDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 271 TLTQEIDFLQQLYEMELSQVQTHVSNTNVVLSMDNNRNL-----DLDSIIAEVKAqyELIAQRSRAEA-----EAWYQTK 340
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWqvvegALDAQLALLKA--AIAARRSGAKAelkalETWYKRD 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 341 YEELqvtaGKHGDNLRDTKNEIAELTRTIQRLQG------------------EADAAKKQCQQLQTAIAEAEQR------ 396
Cdd:pfam12128 760 LASL----GVDPDVIAKLKREIRTLERKIERIAVrrqevlryfdwyqetwlqRRPRLATQLSNIERAISELQQQlarlia 835
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 32567786 397 -GELALKDAQKKLGDLDVALHQAKEDLTRlLRDYQELMN-VKLALDVEIA 444
Cdd:pfam12128 836 dTKLRRAKLEMERKASEKQQVRLSENLRG-LRCEMSKLAtLKEDANSEQA 884
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
132-461 |
5.42e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 132 DPEIQRVRTQereqIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGQNLgvtRNNLEPLfEAYLGSMRSTLDRLQS 211
Cdd:pfam10174 302 ESELLALQTK----LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDAL---RLRLEEK-ESFLNKKTKQLQDLTE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 212 ERGRLDSELRNVQDLVeDFKnkyEDEINkhtaaenefvVLKKDVDAAymgRMDLHGKVGTLTQEIDFLQQLyemelsqvQ 291
Cdd:pfam10174 374 EKSTLAGEIRDLKDML-DVK---ERKIN----------VLQKKIENL---QEQLRDKDKQLAGLKERVKSL--------Q 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 292 THVSNTNVVLSMdnnrnldldsiIAEVKAQYELIAQRSRAEAEAWYQTKYEELQvtagkhgdnlrDTKNEIAELTRTIQR 371
Cdd:pfam10174 429 TDSSNTDTALTT-----------LEEALSEKERIIERLKEQREREDRERLEELE-----------SLKKENKDLKEKVSA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 372 LQGEADAAKKQCQQLQTAIAEAEQRGelALKDAqkKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDV--EIATYRKL 449
Cdd:pfam10174 487 LQPELTEKESSLIDLKEHASSLASSG--LKKDS--KLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTnpEINDRIRL 562
|
330
....*....|..
gi 32567786 450 LESEESRMSGEC 461
Cdd:pfam10174 563 LEQEVARYKEES 574
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-460 |
5.70e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 268 KVGTLTQEIDFLQQ---LYEMELSQVQTHVSN---TNVVLSMDNNRNLDLDSIiAEVKAQYELiAQRSRAEAEAWYQTKY 341
Cdd:COG3206 169 RREEARKALEFLEEqlpELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 342 EELQVTAGKHGDNLRDT-----KNEIAELTRTIQRLQG-------EADAAKKQCQQLQTAIAEAEQRGELALKD----AQ 405
Cdd:COG3206 247 AQLGSGPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAeleaLQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 32567786 406 KKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKLLE-SEESRMSGE 460
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQrLEEARLAEA 382
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-414 |
7.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 196 EAYLGSMRSTLDRLQSERGRLDSELRNVQDLVEDFKNKYEDEINKHTAAENEFVVLKKDVDAAymgrmdlhgkvgtlTQE 275
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA--------------EAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 276 IDFLQQLYEMELSQVQTH---VSNTNVVLSMDN-----NRNLDLDSIiaeVKAQYELIAQRSRAEAEAwyqtkyEELQVT 347
Cdd:COG3883 81 IEERREELGERARALYRSggsVSYLDVLLGSESfsdflDRLSALSKI---ADADADLLEELKADKAEL------EAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32567786 348 AGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGELALKDAQKKLGDLDVA 414
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
160-428 |
9.61e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 160 VRFLEQQNKVLETKWALLQEQGQNLGVTRNNLEPLFEAYlgsmRSTLDRLQSERGRLDSELRNVQD-LVEDFKNkYEDEI 238
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTY----NKNIEEQRKKNGENIARKQNKYDeLVEEAKT-IKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 239 NKHTAAENEFVVLKKDVDAAY----MGRMDLHGKVGTLTQEIDFLQQLYEMELSQVQthvsntnvvLSMDNNRNLDLDSI 314
Cdd:PHA02562 237 EELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQ---------ISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 315 IAEVKAQYELIaqrsraeaeawyQTKYEELQVTAGKHGDN---LRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIA 391
Cdd:PHA02562 308 LKELQHSLEKL------------DTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 32567786 392 EAEqrGELA-----LKDAQKKLGDLDVALHQaKEDLTRLLRD 428
Cdd:PHA02562 376 DNA--EELAklqdeLDKIVKTKSELVKEKYH-RGIVTDLLKD 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-456 |
1.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 310 DLDSIIAEVKAQYELIAQRsRAEAEAWYQ---TKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQL 386
Cdd:COG1196 236 ELEAELEELEAELEELEAE-LEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 387 QTAIAEAEQ-----------------RGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQELMNVKLALDVEIATYRKL 449
Cdd:COG1196 315 EERLEELEEelaeleeeleeleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
....*..
gi 32567786 450 LESEESR 456
Cdd:COG1196 395 AAELAAQ 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-456 |
1.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 347 TAGKHGDNLR---------DTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGELALKDAQKKLGDLDVA--- 414
Cdd:COG4913 588 TRHEKDDRRRirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsae 667
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 32567786 415 --LHQAKEDLTRLLRDYQELMnvklALDVEIATYRKLLESEESR 456
Cdd:COG4913 668 reIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEE 707
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
130-454 |
2.04e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 130 EIDPEIQRVRTQE-REQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQ------GQNLGVTR-NNLEPLFEAYLGS 201
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcGTTLGEEKsNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 202 MRSTLDRLQSERGRLDSELRNVQDLVEDFK----NKYEDEINKHTAAENEfvvLKKDVDAayMGRM-DLHGKVGTLTQEI 276
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARAD---LEDIKIK--INELkDKHDKYEEIKNRY 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 277 dflQQLYEMELSQVQTHVSNTNVVLSmdnnrNLDLDSIIA---EVKAQYELIAQRSRaEAEAWYQTKYEELQVTAGKHGD 353
Cdd:PRK01156 556 ---KSLKLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQ-EIEIGFPDDKSYIDKSIREIEN 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 354 ---NLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQtAIAEAEQRGELALKDAQKKLGDLDVALHQAKEDLTRLLRDYQ 430
Cdd:PRK01156 627 eanNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
330 340
....*....|....*....|....
gi 32567786 431 ELMNVKLALDVEIATYRKLLESEE 454
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMK 729
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-458 |
2.41e-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: 39.52 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 339 TKYEELQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRgelaLKDAQKKLG------DLD 412
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQLGnvrnnkEYE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32567786 413 VALHQaKEDLTRLLRDYQELMnvkLALDVEIATYRKLLESEESRMS 458
Cdd:COG1579 93 ALQKE-IESLKRRISDLEDEI---LELMERIEELEEELAELEAELA 134
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
252-428 |
2.94e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 252 KKDVDAAYMGRMDLHGKVGTLTQEIDFLQQLYEMELSQVQTHVSNTNVVLSMDNNRNLDLDSIIAEVKAQYE-LIAQRSR 330
Cdd:pfam15905 151 QKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEkLLEYITE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 331 AEAEAWYQTKYEE----LQVTAGKHGDNLRDTKNEIAELTRTIQRLQGEADAakkQCQQLQTAIAEAEQRGELALKDAQK 406
Cdd:pfam15905 231 LSCVSEQVEKYKLdiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE---KCKLLESEKEELLREYEEKEQTLNA 307
|
170 180
....*....|....*....|..
gi 32567786 407 KLGDLDVALHQAKEDLTRLLRD 428
Cdd:pfam15905 308 ELEELKEKLTLEEQEHQKLQQK 329
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
355-432 |
3.64e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 355 LRDTKNEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGELAL---------------KDAQKKLGDLDVALHQAK 419
Cdd:COG1842 32 IRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALekgredlarealerkAELEAQAEALEAQLAQLE 111
|
90
....*....|...
gi 32567786 420 EDLTRLLRDYQEL 432
Cdd:COG1842 112 EQVEKLKEALRQL 124
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
363-456 |
4.66e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 363 AELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQRGELALKDAQKKLGDLDVALHQAKEDLTRLlrdyqELMNVKL-ALDV 441
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQV-----ELLNQQIaALRR 151
|
90
....*....|....*
gi 32567786 442 EIATYRKLLESEESR 456
Cdd:PRK09039 152 QLAALEAALDASEKR 166
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
214-407 |
8.30e-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: 38.50 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 214 GRLDSELRNVQDLVEDFKNKYED-EINKHTAAENEFV-VLKKDVDaaymgrmDLHGKVGTLTQEI-DFLQQLYEmELSQV 290
Cdd:cd22656 87 GTIDSYYAEILELIDDLADATDDeELEEAKKTIKALLdDLLKEAK-------KYQDKAAKVVDKLtDFENQTEK-DQTAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32567786 291 QTHVSNTNVVLSMDNNRNL--DLDSIIAEVKAQYELIAQRSRA---EAEAWYQTKYEELQV------TAGKHGDNLRDTK 359
Cdd:cd22656 159 ETLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAKLKAkidELKALIADDEAKLAAalrliaDLTAADTDLDNLL 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 32567786 360 NEIAELTRTIQRLQGEADAAKKQCQQLQTAIAEAEQ------RGELALKDAQKK 407
Cdd:cd22656 239 ALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaaiLAKLELEKAIEK 292
|
|
| |
