|
Name |
Accession |
Description |
Interval |
E-value |
| RA_ASPP1 |
cd17224 |
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 1 (ASPP1); ... |
72-154 |
7.06e-61 |
|
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 1 (ASPP1); ASPP1 is a member of the ASPP protein family (Apoptosi-Stimulating Protein of p53) that activates the p53-mediated apoptotic response. ASSP1 functions as a tumor suppressor and coordinates with p53 to protect hematopoietic stem cell (HSC) pool integrity, guarding against hematological malignancies. ASSP1 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins.
Pssm-ID: 340744 Cd Length: 85 Bit Score: 201.75 E-value: 7.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 72 MILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRHE 151
Cdd:cd17224 3 MILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGETGCHLAEVWRGNERPIPYDHMMYEHLQKWGPRREEVKFFLRHE 82
|
...
gi 2462539542 152 DSP 154
Cdd:cd17224 83 DSP 85
|
|
| RA_ASPP1_2 |
cd16125 |
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ... |
72-151 |
6.22e-46 |
|
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 (ASPP) 1 and 2; The ASPP protein (apoptosis-stimulating protein of p53; also called ankyrin repeat-, Src homology 3 domain- and Pro-rich region-containing protein) plays a critical role in regulating apoptosis. The ASPP family consists of three members, ASPP1, ASPP2 and iASPP, all of which bind to p53 and regulate p53-mediated apoptosis. ASPP1 and ASPP2, have a RA domain at their N-terminus and have pro-apoptotic functions, while iASPP is involved in anti-apoptotic responses. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin.
Pssm-ID: 340542 Cd Length: 80 Bit Score: 159.00 E-value: 6.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 72 MILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRHE 151
Cdd:cd16125 1 VILKVYLSDNNQTVTEVPITPETTCQDVVDCCKEPGEENCHLVEVWRGCERPLPEEENPYEILQQWGSHRDEVKFFLRHE 80
|
|
| RA_ASPP2 |
cd17225 |
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ... |
72-151 |
1.99e-39 |
|
Ras-associating (RA) domain found in apoptosis-stimulating protein of p53 protein 2 (ASPP2); ASPP2, also termed Bcl2-binding protein (Bbp), or renal carcinoma antigen NY-REN-51, or tumor suppressor p53-binding protein 2 (53BP2), or p53-binding protein 2 (p53BP2), is a member of ASPP protein family and it functions as a tumor suppressor. ASPP2 binds to p53 and enhances p53-mediated transcription of proapoptotic genes. ASSP2 contains a RA domain at the N-terminus. The RA domain is a ubiquitin-like domain and RA domain-containing proteins are involved in several different functions ranging from tumor suppression to being oncoproteins. All p53 amino acids that are important for ASPP2 binding are mutated in human cancer, and ASPP2 is frequently downregulated in these tumor cells.
Pssm-ID: 340745 Cd Length: 80 Bit Score: 140.71 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 72 MILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRHE 151
Cdd:cd17225 1 MFLTVYLSNNEQHFTEVPITPETTCRDVVELCKEPGETDCHLAEVWRGSERPVADNERMLDVLQQWGAQRNEVRFFLRHE 80
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
548-966 |
9.44e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 73.05 E-value: 9.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 548 GKVPPPIPGVG------KQLPPSYgtyPSPTPLGPGSTSSLER------RKEGSLPRPSAGLPSRQRP--TLLPATGSTP 613
Cdd:PHA03247 2549 GDPPPPLPPAAppaapdRSVPPPR---PAPRPSEPAVTSRARRpdappqSARPRAPVDDRGDPRGPAPpsPLPPDTHAPD 2625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 614 QPGSSQQiqQRISVPPSPTYPPAGPPAFPAGDSKP---ELPLTVAIRPFLADKGSRPQSPRK--GPQTVNSSSIYSMYLQ 688
Cdd:PHA03247 2626 PPPPSPS--PAANEPDPHPPPTVPPPERPRDDPAPgrvSRPRRARRLGRAAQASSPPQRPRRraARPTVGSLTSLADPPP 2703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 689 QATPPKNYQPAAHSALNKSVKAVYGKPVLPSGSTSPSPLPFLHGSLSTGTPQPQPPSESTEKEPEQDGPAAPADGstves 768
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG----- 2778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 769 lprplSPTKLTPIVHSPLRyQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGPniqkllyqrfntLAGGMEGTPFYQP 848
Cdd:PHA03247 2779 -----PPRRLTRPAVASLS-ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGP------------LPPPTSAQPTAPP 2840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 849 SPSQDFMGTLAdvDNGNTNANGNLEELPPAQPTAPLPA-----------EPAPSSDANDNELPSPEPEelicPQTTHQTA 917
Cdd:PHA03247 2841 PPPGPPPPSLP--LGGSVAPGGDVRRRPPSRSPAAKPAaparppvrrlaRPAVSRSTESFALPPDQPE----RPPQPQAP 2914
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462539542 918 EPAEdnnnnvatvpTTEQIPSPVAEAPSPGEEQVPPAPLPPASHPPATS 966
Cdd:PHA03247 2915 PPPQ----------PQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG 2953
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
993-1058 |
4.27e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 62.28 E-value: 4.27e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539542 993 ALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGW 1058
Cdd:COG0666 89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
994-1060 |
4.76e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.89 E-value: 4.76e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539542 994 LLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGA 1060
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
994-1060 |
1.43e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 60.35 E-value: 1.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539542 994 LLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGA 1060
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
995-1056 |
1.69e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 55.89 E-value: 1.69e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462539542 995 LLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFgVNVNAADSD 1056
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG 61
|
|
| RA_RASSF7_like |
cd16123 |
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, ... |
90-150 |
2.06e-09 |
|
Ras-associating (RA) domain found in Ras-association domain family members, RASSF7, RASSF8, RASSF9, and RASSF10; The RASSF family of proteins shares a conserved RalGDS/AF6 Ras association (RA) domain either in the C-terminus (RASSF1-6) or N-terminus (RASSF7-10). RASSF7-10 lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The structural differences between the C-terminus and N-terminus RASSF subgroups have led to the suggestion that they are two distinct families. RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ras proteins are small GTPases that are involved in cellular signal transduction. The N-terminus RASSF proteins are potential Ras effectors that have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia.
Pssm-ID: 340540 Cd Length: 81 Bit Score: 54.94 E-value: 2.06e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539542 90 ITPETTCRDVV-----EFCKEPGEGSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRH 150
Cdd:cd16123 16 VTERTTCQDVIyalaqATGQTNDTGRYVLVERWRGIERPLPPRTRILKVWKAWGEEQSNVQFVLRR 81
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
226-399 |
1.42e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 226 FLKQQERRQQQSISE-----NEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNgNLSAEIERFSAMFQEKKQEVQTAI 300
Cdd:COG3206 161 YLEQNLELRREEARKaleflEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-LLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 301 LRVDQLSQQLEdlkkgklNGFQSYNGKLTGPAAVELKRLYQELQ-------------------IRNQLNQEQNSKLQQQK 361
Cdd:COG3206 240 ARLAALRAQLG-------SGPDALPELLQSPVIQQLRAQLAELEaelaelsarytpnhpdviaLRAQIAALRAQLQQEAQ 312
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462539542 362 ELLNKRNMEVAMMDKRISELRERLYGKKIQLNRVNGTS 399
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| RA |
cd17043 |
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ... |
73-150 |
2.45e-08 |
|
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.
Pssm-ID: 340563 Cd Length: 87 Bit Score: 52.32 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 73 ILTVFLS--NNEQILTEVPITPETTCRDVVEFCKE-----PGEGSCHLAEVW--RGNERPIPFDHMMYEHLQKWGPRREE 143
Cdd:cd17043 1 VLKVYDDdlAPGSAYKSILVSSTTTAREVVQLLLEkygleEDPEDYSLYEVSekQETERVLHDDECPLLIQLEWGPQGTE 80
|
....*..
gi 2462539542 144 VKFFLRH 150
Cdd:cd17043 81 FRFVLKR 87
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
221-397 |
5.26e-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: 57.37 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 221 EQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKiraMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAI 300
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE---LEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 301 LRVDQLSQQLEDLKKGKLNGFQSYNGKLTGPAAVELKRLYQELqirNQLNQEQNsKLQQQKELLNKRnmeVAMMDKRISE 380
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL---EELEEELE-ELQEELERLEEA---LEELREELEE 472
|
170
....*....|....*..
gi 2462539542 381 LRERLYGKKIQLNRVNG 397
Cdd:TIGR02168 473 AEQALDAAERELAQLQA 489
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-414 |
5.28e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 227 LKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAmrgqvdyskimngnlsaEIERFSAMFQEKKQEVQTAILRVDQL 306
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----------------ELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 307 SQQLEDLKKgklngfqsyngkltgpaavELKRLYQELQirnQLNQEQNSKLQQQKEL---LNKRNMEVAMMDKRISELRE 383
Cdd:COG4372 100 QEELESLQE-------------------EAEELQEELE---ELQKERQDLEQQRKQLeaqIAELQSEIAEREEELKELEE 157
|
170 180 190
....*....|....*....|....*....|.
gi 2462539542 384 RLYGKKIQLNRVNGTSSPQSPLSTSGRVAAV 414
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDEL 188
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
220-402 |
8.84e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 220 KEQRLH-----FLKQQERRQQQS---ISENEK-LQKLKERVeaqeNKLKKiramrgQVDYSKIMNGNLSAEIErfsamfq 290
Cdd:TIGR04523 304 KEQDWNkelksELKNQEKKLEEIqnqISQNNKiISQLNEQI----SQLKK------ELTNSESENSEKQRELE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 291 EKKQEVQTAILRVDQLSQQLEDLKKGKLNgfqsyngkltgpaavelkrLYQELQIRNQLNQEQNSK---LQQQKELLNKR 367
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQIND-------------------LESKIQNQEKLNQQKDEQikkLQQEKELLEKE 427
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462539542 368 ----NMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQ 402
Cdd:TIGR04523 428 ierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
990-1060 |
1.05e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 54.96 E-value: 1.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462539542 990 NPLALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGA 1060
Cdd:COG0666 53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
221-385 |
5.40e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 221 EQRLHFLKQQERRQQQSISE-NEKLQKLKERVEAQENKLKKIramrgqvdyskimNGNLSAEIERFSAMfqekKQEVQTA 299
Cdd:COG4372 44 QEELEQLREELEQAREELEQlEEELEQARSELEQLEEELEEL-------------NEQLQAAQAELAQA----QEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 300 ILRVDQLSQQLEDLKKgklngfqsyngkltgpaavELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRIS 379
Cdd:COG4372 107 QEEAEELQEELEELQK-------------------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
....*.
gi 2462539542 380 ELRERL 385
Cdd:COG4372 168 ALEQEL 173
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
469-1000 |
1.13e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 469 DVGPNYGSSRPSASPFVN-----PNDGNWPTLKQNSSSSVKPVQVAGADWKDPSVEGSVKQGTVSSQPVPFSALGPTEKP 543
Cdd:PHA03247 2604 DRGDPRGPAPPSPLPPDThapdpPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP 2683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 544 GIEIGKVP---------PPIPGVGKQLPPSYGTYPSPTPLGPGST-SSLERRKEGSLPRPSAG---LPSRQRPTLLPATG 610
Cdd:PHA03247 2684 RRRAARPTvgsltsladPPPPPPTPEPAPHALVSATPLPPGPAAArQASPALPAAPAPPAVPAgpaTPGGPARPARPPTT 2763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 611 STPQpgSSQQIQQRISVPPSPTYPPAGPPAFPAGDSKPeLPLTVAIRPFLADKGSRPQSPRKGPQTVnsssiysmylqqA 690
Cdd:PHA03247 2764 AGPP--APAPPAAPAAGPPRRLTRPAVASLSESRESLP-SPWDPADPPAAVLAPAAALPPAASPAGP------------L 2828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 691 TPPKNYQPAAhsalnksvkavygkPVLPSGStSPSPLPfLHGSLSTG-------TPQPQPPSESTEKEPEQDGPAAPADG 763
Cdd:PHA03247 2829 PPPTSAQPTA--------------PPPPPGP-PPPSLP-LGGSVAPGgdvrrrpPSRSPAAKPAAPARPPVRRLARPAVS 2892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 764 STVESLPRPLSPTKLTPIVHSPLRYQSDADLEALRR---KLANAPRPLKKRSSITEPEGPGGPNiQKLLYQRFNTLAGGM 840
Cdd:PHA03247 2893 RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpqpPPPPPPRPQPPLAPTTDPAGAGEPS-GAVPQPWLGALVPGR 2971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 841 EGTPFYQPSPSQDFMGTladvdngntnangnleelpPAQPTAPLPAEPAP------SSDANDNElPSPEPEELIcpqtth 914
Cdd:PHA03247 2972 VAVPRFRVPQPAPSREA-------------------PASSTPPLTGHSLSrvsswaSSLALHEE-TDPPPVSLK------ 3025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 915 QTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPgeeqVPPAPLPPASHPPATSTNKRTNLKKPNSErtghglrvrFNPLAL 994
Cdd:PHA03247 3026 QTLWPPDDTEDSDADSLFDSDSERSDLEALDP----LPPEPHDPFAHEPDPATPEAGARESPSSQ---------FGPPPL 3092
|
....*.
gi 2462539542 995 LLDASL 1000
Cdd:PHA03247 3093 SANAAL 3098
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1023-1054 |
1.32e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 45.74 E-value: 1.32e-06
10 20 30
....*....|....*....|....*....|...
gi 2462539542 1023 EGITPLHNAVC-AGHHHIVKFLLDFGVNVNAAD 1054
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
992-1044 |
1.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462539542 992 LALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLL 1044
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
191-368 |
1.54e-06 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 52.22 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 191 RVELT-----LSELQDMAARQQQQIENQQQMLVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQEnKLKKIRAMR 265
Cdd:pfam15964 494 GLELSeskqrLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQE-LTQKMQQME 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 266 GQVD------YSKIMNGN-LSAEIERFSAMFQEKKQEV-QTAILRVDQLSQQLEDLkKGKLNGFQSYNGKLTgPAAVELK 337
Cdd:pfam15964 573 AQHDktvneqYSLLTSQNtFIAKLKEECCTLAKKLEEItQKSRSEVEQLSQEKEYL-QDRLEKLQKRNEELE-EQCVQHG 650
|
170 180 190
....*....|....*....|....*....|..
gi 2462539542 338 RLYQELQIR-NQLNQEQNSKLQQQKELLNKRN 368
Cdd:pfam15964 651 RMHERMKQRlRQLDKHCQATAQQLVQLLSKQN 682
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
164-385 |
1.71e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 164 QTQEQRTQRNVINvpgEKRTENGvgNPRVELT--LSELQDMAA--RQQQQIENQQQMLVAKEQRLhfLKQQERRQQ-QSI 238
Cdd:COG1340 58 EAQELREKRDELN---EKVKELK--EERDELNekLNELREELDelRKELAELNKAGGSIDKLRKE--IERLEWRQQtEVL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 239 S-ENEK--------LQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQ 309
Cdd:COG1340 131 SpEEEKelvekikeLEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539542 310 LEDLKKgKLNGFQSyngkltgpAAVELKRLYQELQIR-NQLNQEQNSKLQQQKELlnKRNMEVAMMDKRISELRERL 385
Cdd:COG1340 211 ADELHK-EIVEAQE--------KADELHEEIIELQKElRELRKELKKLRKKQRAL--KREKEKEELEEKAEEIFEKL 276
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1023-1052 |
2.28e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.89 E-value: 2.28e-06
10 20 30
....*....|....*....|....*....|
gi 2462539542 1023 EGITPLHNAVCAGHHHIVKFLLDFGVNVNA 1052
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
713-967 |
2.40e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 713 GKPVLPSGSTSPSPLPflhgSLSTGTPQPQP-PSES--TEKEPEQDGPAAPADGST----VESLPRPLSPTKLTPIVHS- 784
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAP----DRSVPPPRPAPrPSEPavTSRARRPDAPPQSARPRApvddRGDPRGPAPPSPLPPDTHAp 2624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 785 --PLRYQSDADLEALRRKLANAPRPLKKRSSitepegPGGPNIQKLLYQRFNTLAGGMEGTP-FYQPSPSQDFMGTLADV 861
Cdd:PHA03247 2625 dpPPPSPSPAANEPDPHPPPTVPPPERPRDD------PAPGRVSRPRRARRLGRAAQASSPPqRPRRRAARPTVGSLTSL 2698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 862 dngntnANGNLEELPPA-QPTAPLPAEPAPSSDANDNELPSPEPEELICPQTTHQTAEPAEDnnNNVATVPTTeqipspv 940
Cdd:PHA03247 2699 ------ADPPPPPPTPEpAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGP--ARPARPPTT------- 2763
|
250 260
....*....|....*....|....*..
gi 2462539542 941 AEAPSPGEEQVPPAPLPPASHPPATST 967
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
998-1054 |
2.82e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.65 E-value: 2.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462539542 998 ASLEGEFDLVQRIIYEVEdpSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAAD 1054
Cdd:pfam12796 37 AAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
165-389 |
3.14e-06 |
|
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: 51.26 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 165 TQEQRTQRNVINvpgEKRTENGVGNPRVELTLSELQDMaarqqqqienqqqmLVAKEQRLHFLKQQER----RQQQSISE 240
Cdd:pfam05483 330 TEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEEL--------------LRTEQQRLEKNEDQLKiitmELQKKSSE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 241 NEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEI----ERFSAMFQEKKQEVQ------TAILRVDQ-LSQQ 309
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELkgkeQELIFLLQAREKEIHdleiqlTAIKTSEEhYLKE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 310 LEDLKKgKLNGFQSYNGKLTGPA---AVELKRLYQE-----LQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKR--IS 379
Cdd:pfam05483 473 VEDLKT-ELEKEKLKNIELTAHCdklLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRdeLE 551
|
250
....*....|
gi 2462539542 380 ELRERLYGKK 389
Cdd:pfam05483 552 SVREEFIQKG 561
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
219-384 |
4.38e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFLKQQERRQQQsisENEKLQKLKERVEAQ--ENKLKKIRAMRGQVDYSKIMNGNLsAEIERFSAMFQEKKQEV 296
Cdd:pfam13868 49 MEEERERALEEEEEKEEE---RKEERKRYRQELEEQieEREQKRQEEYEEKLQEREQMDEIV-ERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 297 QTAILR-VDQLSQQLEDLKKGKlngfqsyngkltgpaAVELKRLyqELQIR---NQLNQEQNSKLQQQKELLNKRNMEVA 372
Cdd:pfam13868 125 QRQLREeIDEFNEEQAEWKELE---------------KEEEREE--DERILeylKEKAEREEEREAEREEIEEEKEREIA 187
|
170
....*....|..
gi 2462539542 373 MMDKRISELRER 384
Cdd:pfam13868 188 RLRAQQEKAQDE 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
169-365 |
5.91e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 169 RTQRNVINVPGEKRTENGvgnprvelTLSELQD--MAARQQqqienqqqmLVAKEQRLHFLKQQERRQQQSISE---NEK 243
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQ--------QLSELESqlAEARAE---------LAEAEARLAALRAQLGSGPDALPEllqSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 244 LQKLKERVEAQENKLK-----------KIRAMRGQVDyskIMNGNLSAEIERfsaMFQEKKQEVQTAILRVDQLSQQLED 312
Cdd:COG3206 265 IQQLRAQLAELEAELAelsarytpnhpDVIALRAQIA---ALRAQLQQEAQR---ILASLEAELEALQAREASLQAQLAQ 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462539542 313 LKKgKLNGFQSyngkltgpAAVELKRLYQELQIRNQ-----LNQEQNSKLQQQKELLN 365
Cdd:COG3206 339 LEA-RLAELPE--------LEAELRRLEREVEVARElyeslLQRLEEARLAEALTVGN 387
|
|
| RA_RASSF8 |
cd16134 |
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); ... |
90-153 |
8.31e-06 |
|
Ras-associating (RA) domain found in N-terminal Ras-association domain family 8 (RASSF8); RASSF8, also termed carcinoma-associated protein HOJ-1, is a member of the N-terminus RASSF7-10 protein family. RASSF7-10 has an RA-domain at the N-terminus and lacks a conserved SARAH (Salvador/RASSF/Hpo) motif adjacent to the RA domain that is found in members of the RASSF1-6 family. The RA domain of N-terminal RASSF proteins family has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin. RASSF8 has been described as a potential tumor suppressor. RASSF8 might have a role in the regulation of cell-cell adhesion and cell growth.
Pssm-ID: 340551 Cd Length: 82 Bit Score: 45.12 E-value: 8.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539542 90 ITPETTCRDVV-EFCKEPGE-GSCHLAEVWRGNERPIPFDHMMYEHLQKWGPRREEVKFFLRHEDS 153
Cdd:cd16134 16 VTEVTTCQEVViALAQATGRtGRFTLIEKWRNTERLLAPHENPLKVLNKWGQYASDVQFILRRTGP 81
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
494-978 |
1.27e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 49.70 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 494 TLKQNSSSSVKPVQVAGADwkdPSVEGSVKQGTVSSQPVPFSALG-PTEKPGIEiGKVPPP---IPGVGKQLP------- 562
Cdd:PRK10263 328 TATQSWAAPVEPVTQTPPV---ASVDVPPAQPTVAWQPVPGPQTGePVIAPAPE-GYPQQSqyaQPAVQYNEPlqqpvqp 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 563 --PSYGTYPSPTPLGPGSTSSLERRKEGSLPRPSAGLPSRQRPTLLPATGSTPQPGSSQQIQQRISVPPSPTYPPAGPPA 640
Cdd:PRK10263 404 qqPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQP 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 641 FPAGDSKPELPLTVAIRPF---------LADKGSRPQ-----------SPRKGPQTVNSSSiySMYLQQATPPKNYQPAA 700
Cdd:PRK10263 484 VEQQPVVEPEPVVEETKPArpplyyfeeVEEKRAREReqlaawyqpipEPVKEPEPIKSSL--KAPSVAAVPPVEAAAAV 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 701 --------HSALNKSVKAVYGKPVLpSGSTSPSPLPFLHGSLSTGTPQPQPPSESTEKEPEQDGPAAP------------ 760
Cdd:PRK10263 562 splasgvkKATLATGAAATVAAPVF-SLANSGGPRPQVKEGIGPQLPRPKRIRVPTRRELASYGIKLPsqraaeekarea 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 761 ---------------ADGSTVESLPRPLSPTKL----TPIVHSPLRYQSDADLEA---LRRKLANAPrplKKRSSITEPE 818
Cdd:PRK10263 641 qrnqydsgdqynddeIDAMQQDELARQFAQTQQqrygEQYQHDVPVNAEDADAAAeaeLARQFAQTQ---QQRYSGEQPA 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 819 GPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSpsqdfmgtLADVDNGNTNANGNLEELPPAQPTAPLPAEPAPSSdandne 898
Cdd:PRK10263 718 GANPFSLDDFEFSPMKALLDDGPHEPLFTPI--------VEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQ------ 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 899 lPSPEPEELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAPLPPAS--HPPATSTNKRTNLKKP 976
Cdd:PRK10263 784 -PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQDTllHPLLMRNGDSRPLHKP 862
|
..
gi 2462539542 977 NS 978
Cdd:PRK10263 863 TT 864
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1023-1052 |
1.42e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 42.63 E-value: 1.42e-05
10 20 30
....*....|....*....|....*....|
gi 2462539542 1023 EGITPLHNAVCAGHHHIVKFLLDFGVNVNA 1052
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
219-391 |
1.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRamrgqvdyskimngnlsAEIERFSAMFQEKKQEVQT 298
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ-----------------AELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 299 AILRVDQLSQQLEDLKKgklngfqsyngkltgpaavELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRI 378
Cdd:COG4372 113 LQEELEELQKERQDLEQ-------------------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170
....*....|...
gi 2462539542 379 SELRERLYGKKIQ 391
Cdd:COG4372 174 QALSEAEAEQALD 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-522 |
1.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFLKQQERRQQQSISE-NEKLQKLKERVEAQENKLKK-IRAMR---GQVDYSKIM--NGNLSAEIERFSAM--- 288
Cdd:COG3883 48 ELNEEYNELQAELEALQAEIDKlQAEIAEAEAEIEERREELGErARALYrsgGSVSYLDVLlgSESFSDFLDRLSALski 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 289 -----------------FQEKKQEVQTAILRVDQLSQQLEDLKKgKLNGFQSyngkltgpaavELKRLYQELQIRNQLNQ 351
Cdd:COG3883 128 adadadlleelkadkaeLEAKKAELEAKLAELEALKAELEAAKA-ELEAQQA-----------EQEALLAQLSAEEAAAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 352 EQNSKLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSAGSFPVlGD 431
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAA-GA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 432 PIKPQSLSIASNAAHGRSKSDGHSKPRVTSSWTVSDLDVGPNYGSSRPSASPFVNPNDGNWPTLKQNSSSSVKPVQVAGA 511
Cdd:COG3883 275 GAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGG 354
|
330
....*....|.
gi 2462539542 512 DWKDPSVEGSV 522
Cdd:COG3883 355 GGGSSSGGGGG 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
217-385 |
2.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 217 LVAKEQRLHFLKQQERRQQQSISENEK-LQKLKERVEAQENKLKKIRAMRGQVDYSKIMNgNLSAEIErfsamFQEKKQE 295
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKeIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE-ALQKEIE-----SLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 296 V-QTAIL----RVDQLSQQLEDLKKgklngfqsyngkltgpaavELKRLYQEL-QIRNQLNQEQNSKLQQQKELLNKRNM 369
Cdd:COG1579 107 DlEDEILelmeRIEELEEELAELEA-------------------ELAELEAELeEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|....*.
gi 2462539542 370 EVAMMDKRISELRERL 385
Cdd:COG1579 168 LAAKIPPELLALYERI 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
284-396 |
4.23e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 284 RFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKgKLNGFQSyngkltgpaavELKRLYQELQIRNQLNQEQNSKLQQQKEL 363
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLRE-ELEQARE-----------ELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110
....*....|....*....|....*....|...
gi 2462539542 364 LNKRNMEVAMMDKRISELRERLYGKKIQLNRVN 396
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
667-991 |
6.65e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.22 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 667 PQSPRKGPqTVNSSSIYSMYLQQATPPKNYQPA---AHSALNKSVKAVYGKPVLPSGSTS------PSPLPFLHGSLSTG 737
Cdd:pfam05109 425 PESTTTSP-TLNTTGFAAPNTTTGLPSSTHVPTnltAPASTGPTVSTADVTSPTPAGTTSgaspvtPSPSPRDNGTESKA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 738 TPQPQPPSESTEKEPEQDGPAAPADGSTVESLPRPLSPTKLTPIVHSPLRyQSDADLEALRRKLANAPRPLKKRSSITEP 817
Cdd:pfam05109 504 PDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTP-NATSPTPAVTTPTPNATIPTLGKTSPTSA 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 818 EGPGGPNIQKLLY-------QRFNTLAGGMEGTPFYQpSPSQDFMGTLADVDNGNTNANGNLEELPPAQPTAPLPAEPAP 890
Cdd:pfam05109 583 VTTPTPNATSPTVgetspqaNTTNHTLGGTSSTPVVT-SPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSD 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 891 SSDANDNELPSPEPE--ELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPS--PGEEQV----PP----APLPP 958
Cdd:pfam05109 662 NSTSHMPLLTSAHPTggENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTStkPGEVNVtkgtPPknatSPQAP 741
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462539542 959 ASH----PPATSTNKRTNLKKPNSERTGHGLRVRFNP 991
Cdd:pfam05109 742 SGQktavPTVTSTGGKANSTTGGKHTTGHGARTSTEP 778
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
663-972 |
6.96e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 663 KGSRPQSPRKGPQTVNSSSIysmyLQQATPPKNYQPAAHSALNKsvkavygKPVLPSGSTSPSPLPFLHGSLSTGTPQpQ 742
Cdd:PTZ00449 538 KESDEPKEGGKPGETKEGEV----GKKPGPAKEHKPSKIPTLSK-------KPEFPKDPKHPKDPEEPKKPKRPRSAQ-R 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 743 PPSESTEKEPEQ-DGPAAPADGSTVESLPRPLSPTKltPIvhSPLRYQSdadlealrrklanaPRPLKKRSSITEPEGPG 821
Cdd:PTZ00449 606 PTRPKSPKLPELlDIPKSPKRPESPKSPKRPPPPQR--PS--SPERPEG--------------PKIIKSPKPPKSPKPPF 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 822 GPNIQKLLYQRFNTLAggmegtpfyqpSPSQDFMGTLADVDNGNTNANGNLEELPPAQPTAPlpaEPAPSSDANDNELPS 901
Cdd:PTZ00449 668 DPKFKEKFYDDYLDAA-----------AKSKETKTTVVLDESFESILKETLPETPGTPFTTP---RPLPPKLPRDEEFPF 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 902 PEPEELICPQTTH-QTAEPAEDNNNNVATVP--------TTEQIPSP--VAEAPSPGEEQVPP------APLPPASHPPA 964
Cdd:PTZ00449 734 EPIGDPDAEQPDDiEFFTPPEEERTFFHETPadtplpdiLAEEFKEEdiHAETGEPDEAMKRPdspsehEDKPPGDHPSL 813
|
....*...
gi 2462539542 965 TSTNKRTN 972
Cdd:PTZ00449 814 PKKRHRLD 821
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
221-387 |
8.04e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 221 EQRLHFLKQQERRQQqsiseneKLQKLKERVEAQENKLKKIRAmrgqvDYSKIMNGNLSAEIERFSAMFQEKKQEvqtai 300
Cdd:PRK11281 66 EQTLALLDKIDRQKE-------ETEQLKQQLAQAPAKLRQAQA-----ELEALKDDNDEETRETLSTLSLRQLES----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 301 lRVDQLSQQLEDLKKgKLNgfqSYNGKL----TGPAAVE------LKRLyqeLQIRNQLNQEQNSKLQQQKELLNKRNME 370
Cdd:PRK11281 129 -RLAQTLDQLQNAQN-DLA---EYNSQLvslqTQPERAQaalyanSQRL---QQIRNLLKGGKVGGKALRPSQRVLLQAE 200
|
170
....*....|....*..
gi 2462539542 371 VAMMDKRISELRERLYG 387
Cdd:PRK11281 201 QALLNAQNDLQRKSLEG 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
217-382 |
8.40e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 217 LVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFsAMFQEKKQEV 296
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL-EELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 297 QTAILRVDQLSQQLEDLKkgklNGFQSYNGKLTGPAAVELKRL---YQELQIRNQLNQEQNSKLQQQKELLNKR------ 367
Cdd:COG4717 159 RELEEELEELEAELAELQ----EELEELLEQLSLATEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEEleqlen 234
|
170
....*....|....*
gi 2462539542 368 NMEVAMMDKRISELR 382
Cdd:COG4717 235 ELEAAALEERLKEAR 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
220-383 |
9.79e-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: 46.55 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 220 KEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKL-----------------------------------KKIRAM 264
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELnllekeklniqknidkiknkllklelllsnlkkkiQKNKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 265 RGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKK---GKLNGFQSYNGKLTgpaavELKRLYQ 341
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsEKQKELEQNNKKIK-----ELEKQLN 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462539542 342 ELQI-----RNQLNQEQNSKL-----QQQKELLNKRNmEVAMMDKRISELRE 383
Cdd:TIGR04523 292 QLKSeisdlNNQKEQDWNKELkselkNQEKKLEEIQN-QISQNNKIISQLNE 342
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
558-966 |
1.08e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 46.30 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 558 GKQLPPSYGTYPSPTPLGPGSTSSLERRKEGSLPRPSAglpSRQRPTLLPATGSTPQPGSSQQIQQRISVPPSPTYPPAG 637
Cdd:pfam03154 43 GRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSA---KRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 638 PPAFPAGDSKpelpltVAIRPFLADKGSRPQSPR-KGPQTVNS---SSIYSMYLQQATPPKNYQ--PAAHSALNKSVKAV 711
Cdd:pfam03154 120 SSDGRSVNDE------GSSDPKDIDQDNRSTSPSiPSPQDNESdsdSSAQQQILQTQPPVLQAQsgAASPPSPPPPGTTQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 712 YGKPVLPSGSTSPSPLPFLHGSLSTGTPQPQ-PPSESTEKEPEQDGPAAPADGSTVESLPRPLSPTKLTPIVHSPlryqs 790
Cdd:pfam03154 194 AATAGPTPSAPSVPPQGSPATSQPPNQTQSTaAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQ----- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 791 dadlEALRRKLANAPRPLKKRSSITEPEGPGGPniqkLLYQRFNTLAGGMEGTPFYQPSPSQDFMGTLADVDNGNTNANG 870
Cdd:pfam03154 269 ----PSLHGQMPPMPHSLQTGPSHMQHPVPPQP----FPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 871 NLEELPPAQ---------PTAPLPAEPAPSSDANDNELPSPEPEEL---------ICPQTTHQTAEPAEDNNNNVATVPT 932
Cdd:pfam03154 341 REQPLPPAPlsmphikppPTTPIPQLPNPQSHKHPPHLSGPSPFQMnsnlppppaLKPLSSLSTHHPPSAHPPPLQLMPQ 420
|
410 420 430
....*....|....*....|....*....|....
gi 2462539542 933 TEQIPSPVAEapSPGEEQVPPAPLPPASHPPATS 966
Cdd:pfam03154 421 SQQLPPPPAQ--PPVLTQSQSLPPPAASHPPTSG 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
213-425 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 213 QqqmlvakEQRLHFLKQQERRQQQSISENEK-LQKLKERVEAQENKLKK-IRAM--RGQVDYSK-IMNGNLSAEIERFSA 287
Cdd:COG4942 67 L-------ARRIRALEQELAALEAELAELEKeIAELRAELEAQKEELAElLRALyrLGRQPPLAlLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 288 MFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNgfqsyngkltgpAAVELKRLYQELQI-RNQLNQEQnsklQQQKELLNK 366
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEA------------ERAELEALLAELEEeRAALEALK----AERQKLLAR 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539542 367 RNMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSAGS 425
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSGR 262
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
514-964 |
1.34e-04 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 46.20 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 514 KDPSVEGSVKQGTVSSQPVPFSALG---PTEKPGIEIGKVPPPIPgvgKQLP-PSYGTYPSPTPLGPGSTSSLERRKEGS 589
Cdd:PHA03377 372 EDTGRQGSDVELESSDDELPYIDPNmepVQQRPVMFVSRVPWRKP---RTLPwPTPKTHPVKRTLVKTSGRSDEAEQAQS 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 590 LPRpsaglpsrqrptllpatgstpQPGSSQQIqqriSVPPSPTYPPAGPPAFPAGDSKPELPLTVAIRPfladkGSRPQS 669
Cdd:PHA03377 449 TPE---------------------RPGPSDQP----SVPVEPAHLTPVEHTTVILHQPPQSPPTVAIKP-----APPPSR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 670 PRKGPQTVNSSSIYSMYLQQATPPKNY--QPAAHSALNKSVKAVYGK--------PVLPSGSTSPSPLPFLHGSLSTGTP 739
Cdd:PHA03377 499 RRRGACVVYDDDIIEVIDVETTEEEESvtQPAKPHRKVQDGFQRSGRrqkratppKVSPSDRGPPKASPPVMAPPSTGPR 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 740 QPQPPSEST-EKEPEQDGP--AAPADGSTVESLPRPLSPTKLTPIVHSPLRYQsdadlEALRRKLANAPRPLKKRSSITE 816
Cdd:PHA03377 579 VMATPSTGPrDMAPPSTGPrqQAKCKDGPPASGPHEKQPPSSAPRDMAPSVVR-----MFLRERLLEQSTGPKPKSFWEM 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 817 PEGPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSpsqdfMGTLADVDNGNTNANgNLEELPPAQPTAPLPAEPAPSSDAND 896
Cdd:PHA03377 654 RAGRDGSGIQQEPSSRRQPATQSTPPRPSWLPS-----VFVLPSVDAGRAQPS-EESHLSSMSPTQPISHEEQPRYEDPD 727
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462539542 897 NELpSPEPEELICPQTTHQTAEPAEDNnnnvatvPTTEQIPSPVAEAPSPgeeqvPPAPLPPASHPPA 964
Cdd:PHA03377 728 DPL-DLSLHPDQAPPPSHQAPYSGHEE-------PQAQQAPYPGYWEPRP-----PQAPYLGYQEPQA 782
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
227-405 |
1.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 227 LKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQvdyskimngnLSAEIERFSAMFQEKKQEVQTAILRVDQL 306
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ----------LEAQIAELQSEIAEREEELKELEEQLESL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 307 SQQLEDLKKGKlngfqsyngkltgpAAVELKRLYQELqirNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRISELRERLY 386
Cdd:COG4372 163 QEELAALEQEL--------------QALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
170
....*....|....*....
gi 2462539542 387 GKKIQLNRVNGTSSPQSPL 405
Cdd:COG4372 226 SLEAKLGLALSALLDALEL 244
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
1012-1060 |
1.68e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2462539542 1012 YEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGA 1060
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
1026-1060 |
1.94e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.94e-04
10 20 30
....*....|....*....|....*....|....*
gi 2462539542 1026 TPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGA 1060
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
219-385 |
2.13e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 45.05 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFLKQQERRQQQSiSENEKLQKLKERVEAQEnklKKIRAMRGQVDYSkimngnlsaeierfsamfqEKKQEVQT 298
Cdd:pfam15742 92 IRELELEVLKQAQSIKSQN-SLQEKLAQEKSRVADAE---EKILELQQKLEHA-------------------HKVCLTDT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 299 AILRVDQLSQQLEDLKKgklngfqsyngkltgpAAVELKRLYQELQ-IRNQLNQEQNSKLQQQKELLNKRN---MEVAMM 374
Cdd:pfam15742 149 CILEKKQLEERIKEASE----------------NEAKLKQQYQEEQqKRKLLDQNVNELQQQVRSLQDKEAqleMTNSQQ 212
|
170
....*....|.
gi 2462539542 375 DKRISELRERL 385
Cdd:pfam15742 213 QLRIQQQEAQL 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
217-391 |
2.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 217 LVAKEQRLHFLKQQERRQQQSISE----NEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFsamfQEK 292
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREineiSSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKL----EEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 293 KQEVQTailRVDQLSQQLEDLKKgKLNGFQSYNGKLTgpAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVA 372
Cdd:PRK03918 261 IRELEE---RIEELKKEIEELEE-KVKELKELKEKAE--EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170
....*....|....*....
gi 2462539542 373 MMDKRISELRERLygKKIQ 391
Cdd:PRK03918 335 EKEERLEELKKKL--KELE 351
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
217-385 |
2.33e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 217 LVAKEQRLHFLKQQERRQQQSIseNEKLQKLKErveaQENKL-KKIRAMRGQVDYskimngnLSAEIERFSAMFQEKKQE 295
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDEL--NEELKELAE----KRDELnAQVKELREEAQE-------LREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 296 VQTAILRVDQLSQQLEDLKKgklngfQSYNGKLTGPAAVELKRLYQELQirnqlNQEQNSKL--QQQKELLNKrnmevam 373
Cdd:COG1340 80 RDELNEKLNELREELDELRK------ELAELNKAGGSIDKLRKEIERLE-----WRQQTEVLspEEEKELVEK------- 141
|
170
....*....|..
gi 2462539542 374 mdkrISELRERL 385
Cdd:COG1340 142 ----IKELEKEL 149
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1005-1057 |
2.63e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 44.66 E-value: 2.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462539542 1005 DLVQRIIYEVEDPSKPNDEGITPLHNAV--CAGHHHIVKFLLDFGVNVNAADSDG 1057
Cdd:PHA03100 87 EIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDG 141
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
227-606 |
3.02e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.04 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 227 LKQQERRQQQSISeneKLQKLKERVEaqeNKLKKIRAMR-GQVDYSKIMNGNLSAEIE-----RFSAMFQEKKQEVQTAI 300
Cdd:PTZ00108 990 LDLYKKRKEYLLG---KLERELARLS---NKVRFIKHVInGELVITNAKKKDLVKELKklgyvRFKDIIKKKSEKITAEE 1063
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 301 LRVDQL-SQQLEDLKKGKLNGFQSYNGKLTGPaaveLKRLYQElQIRNqLNQEQNSKLQQQKELLNKrnmEVAMMDKR-I 378
Cdd:PTZ00108 1064 EEGAEEdDEADDEDDEEELGAAVSYDYLLSMP----IWSLTKE-KVEK-LNAELEKKEKELEKLKNT---TPKDMWLEdL 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 379 SELRERL--YGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSAG-SFPVLGDPIKPQSLSIASNAAHGRSKSDGHS 455
Cdd:PTZ00108 1135 DKFEEALeeQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKkSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 456 KPRVTSSWTVSDLDVGPNYGSSRPSASPFVNPNDGNWPTLKQNSSSSVKPVQVAGADWKDPSVEGSVKqgtvSSQPVPFS 535
Cdd:PTZ00108 1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQ----YSPPPPSK 1290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462539542 536 ALGPTEKPGieIGKVPPPIPGVGKQLPPSYGTYPSPTP--LGPGSTSSLERRKEGSLPRPSAGLPSRQRPTLL 606
Cdd:PTZ00108 1291 RPDGESNGG--SKPSSPTKKKVKKRLEGSLAALKKKKKseKKTARKKKSKTRVKQASASQSSRLLRRPRKKKS 1361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-381 |
3.10e-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: 45.06 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 220 KEQRLHFLKQQERRQQQSISENEklQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTA 299
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIE--QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 300 ILRVDQLSQQLEDLKKGKLngfqsyngkltgpaavELKRLYQELQIRnqlNQEQNSKLQQQKELLNKRNMEVAMMDKRIS 379
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERD----------------ELEAQLRELERK---IEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
..
gi 2462539542 380 EL 381
Cdd:TIGR02169 935 EI 936
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
219-394 |
3.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFLKQQERRQQQSISENEKLQK-LKERVEAQENKL----KKIRAMRGQVDyskimngNLSAEIERFSAmfQEKK 293
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKaLLKQLAALERRIaalaRRIRALEQELA-------ALEAELAELEK--EIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 294 QEVQTAILRvDQLSQQLEDLKKgklNGFQSYNGKLTGPA-AVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVA 372
Cdd:COG4942 95 LRAELEAQK-EELAELLRALYR---LGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180
....*....|....*....|..
gi 2462539542 373 MMDKRISELRERLYGKKIQLNR 394
Cdd:COG4942 171 AERAELEALLAELEEERAALEA 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-362 |
3.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 195 TLSELQDMAARQQQQIENQQQMLVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDyskim 274
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA----- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 275 ngNLSAEIER-FSAMFQEKKQEVQTAILRVDQLSQQLEDLKKgklngfqsyngkltgpaavELKRLYQEL-QIRNQLNQE 352
Cdd:COG4717 174 --ELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEE-------------------ELEEAQEELeELEEELEQL 232
|
170
....*....|
gi 2462539542 353 QNSKLQQQKE 362
Cdd:COG4717 233 ENELEAAALE 242
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
527-823 |
3.51e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 44.67 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 527 VSSQPVPFSALGPtekpgIEIGKVPPPIPGVGKQLPPSYGTYPSPTPLG---PGSTSSLERRKEGSLPR--PSAGLPSRQ 601
Cdd:PHA03378 559 VHDQLLPAPGLGP-----LQIQPLTSPTTSQLASSAPSYAQTPWPVPHPsqtPEPPTTQSHIPETSAPRqwPMPLRPIPM 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 602 RP-TLLPATGSTPQPGSSQQIQQRISVPPSPTYPPAGPPAFPAGDSKPELPLTVAIRPFLADKGSR---PQSPRKGPQTV 677
Cdd:PHA03378 634 RPlRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRaptPMRPPAAPPGR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 678 N---SSSIYSMYLQQATPPKNYQPAAHSALNKSVKAVYGKPVLPSGSTSPSPLPFLHGSLSTGTPQPQPPSestekEPEQ 754
Cdd:PHA03378 714 AqrpAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPP-----APQQ 788
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539542 755 DGPAAPADGSTVESLPrplSPTKLTPIVHSPLRYQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGP 823
Cdd:PHA03378 789 RPRGAPTPQPPPQAGP---TSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPSLKKPAALERQAAAGP 854
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
403-763 |
4.66e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 44.18 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 403 SPLSTSGRVAAVGPYIQVPSAGSFPVLGDPIKPQSLSIASNAAHGRSKSDGHSKPRVTSSWTVSDLDVGPNYGSSRP--S 480
Cdd:pfam17823 99 EPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPrtA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 481 ASPFVNPNDGNWPTLKQNSSSSVKPVQVAGADwkdPSVEGSVKQGTVSSQPVPFSALGPTEKPGIEIGKVPPPIPGVGKQ 560
Cdd:pfam17823 179 ASSTTAASSTTAASSAPTTAASSAPATLTPAR---GISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALAT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 561 LPPSYGTYPSPTplGPGSTSSLERRKegslPRPSAGLPSRQRpTLLPATGSTPQP-GSSQQI---QQRISVPPSPTyppa 636
Cdd:pfam17823 256 LAAAAGTVASAA--GTINMGDPHARR----LSPAKHMPSDTM-ARNPAAPMGAQAqGPIIQVstdQPVHNTAGEPT---- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 637 gppafpagdskpelpltvairPFLADKGSRPQSPRKGPQTvNSSSIYSMYLQQATPPKNYQPAAHSALNKSVKAVygkpv 716
Cdd:pfam17823 325 ---------------------PSPSNTTLEPNTPKSVAST-NLAVVTTTKAQAKEPSASPVPVLHTSMIPEVEAT----- 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462539542 717 lpSGSTSPSPLPFLHGSLSTGTPQpQPPSESTEKEPEQD--GPAAPADG 763
Cdd:pfam17823 378 --SPTTQPSPLLPTQGAAGPGILL-APEQVATEATAGTAsaGPTPRSSG 423
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-393 |
5.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 247 LKERVEAQENKLKKIRAMRGqvdyskIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKgKLNGFQSYNG 326
Cdd:COG4717 47 LLERLEKEADELFKPQGRKP------ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 327 KLTgpAAVELKRLYQEL-QIRNQLNQEQNS--KLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQLN 393
Cdd:COG4717 120 KLE--KLLQLLPLYQELeALEAELAELPERleELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
268-366 |
7.18e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.02 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 268 VDYSKIMNgnLSAEIERFSAMFQEKKQEVQTAIlrvDQLSQQLEDLKKgKLNGFQSYNGKLTGPAAVELKRLYQELQirn 347
Cdd:pfam03938 5 VDMQKILE--ESPEGKAAQAQLEKKFKKRQAEL---EAKQKELQKLYE-ELQKDGALLEEEREEKEQELQKKEQELQ--- 75
|
90 100
....*....|....*....|
gi 2462539542 348 QLNQEQNSKLQQ-QKELLNK 366
Cdd:pfam03938 76 QLQQKAQQELQKkQQELLQP 95
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-394 |
7.23e-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: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 221 EQRLHFLKQQERRQQQSISE-NEKLQKLKERVEAQENKLKKIRAMRgQVDYSKIMNGNLSAEIERF----------SAMF 289
Cdd:COG4913 609 RAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELeaelerldasSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 290 QEKKQEVQTAILRVDQLSQQLEDLKK--GKLNGfqsyngkltgpaavELKRLYQEL-QIRNQLNQEQNSKLQQQKELLNK 366
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGeiGRLEK--------------ELEQAEEELdELQDRLEAAEDLARLELRALLEE 753
|
170 180
....*....|....*....|....*...
gi 2462539542 367 RNmEVAMMDKRISELRERLYGKKIQLNR 394
Cdd:COG4913 754 RF-AAALGDAVERELRENLEERIDALRA 780
|
|
| PRK08691 |
PRK08691 |
DNA polymerase III subunits gamma and tau; Validated |
848-960 |
7.42e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236333 [Multi-domain] Cd Length: 709 Bit Score: 43.54 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 848 PSPSQDFMGTL------ADVDNGNTNANGNLEELPPAQPTAPLPAEPApssdANDNELPSPEPEELICP-QTTHQTAEPA 920
Cdd:PRK08691 342 PDEYAGFMMTLlrmlafAPLAAASCDANAVIENTELQSPSAQTAEKET----AAKKPQPRPEAETAQTPvQTASAAAMPS 417
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462539542 921 EDNNNNVATVPTTEQIPsPVAEAPSPGEEQVPPAPLPPAS 960
Cdd:PRK08691 418 EGKTAGPVSNQENNDVP-PWEDAPDEAQTAAGTAQTSAKS 456
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
876-967 |
7.94e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 876 PPAQPTAPLPAEPAPSSDANDNELPSPEPEELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAP 955
Cdd:PRK07764 403 AAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAP 482
|
90
....*....|..
gi 2462539542 956 LPPASHPPATST 967
Cdd:PRK07764 483 APPAAPAPAAAP 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
179-393 |
9.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 179 GEKRTENGVGNPRVELtlSELQDMAARQQQQIENQQQMLVAK---EQRLHFLKQQERRQQQSISEnekLQKLKERVEAQE 255
Cdd:TIGR02169 658 GSRAPRGGILFSRSEP--AELQRLRERLEGLKRELSSLQSELrriENRLDELSQELSDASRKIGE---IEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 256 NKLK-KIRAMRGQVDYskimngnLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLK--------------KGKLNG 320
Cdd:TIGR02169 733 EKLKeRLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsripeiqaeLSKLEE 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539542 321 FQSYNGKLTGPAAVELKRLYQELQirnQLNQEQNSKLQQQKELLNKRNM---EVAMMDKRISELRERLYGKKIQLN 393
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKE---YLEKEIQELQEQRIDLKEQIKSiekEIENLNGKKEELEEELEELEAALR 878
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
220-366 |
9.33e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 220 KEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRgqvdySKIMngNLSAEIERFsamfqeKKQEVQTA 299
Cdd:TIGR00606 216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL-----SKIM--KLDNEIKAL------KSRKKQME 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 300 ILRvDQLSQQLEDLKKG---KLNGFQSYNGKLTGPAAVELKRLYQELQIRNQLNQEQNsklQQQKELLNK 366
Cdd:TIGR00606 283 KDN-SELELKMEKVFQGtdeQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN---QEKTELLVE 348
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
157-394 |
9.92e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 157 NSEQGGRQTQEQRTQRNVinvpGEKRTENGVGNPRVELTLSELQDMAARQQQQIENQQQmLVAKEQRLHFLKQQERRQQQ 236
Cdd:pfam05557 110 KNELSELRRQIQRAELEL----QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS-LAEAEQRIKELEFEIQSQEQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 237 SISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSA-MFQEKKQEVQTAILRVDqLSQQLEDLKK 315
Cdd:pfam05557 185 DSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkLEREEKYREEAATLELE-KEKLEQELQS 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 316 GKlNGFQSYNGKLTGPAAveLKRLYQELQIRNQLNQEQNS--------------KLQQQKELLNKRNMEVAMMDKRISEL 381
Cdd:pfam05557 264 WV-KLAQDTGLNLRSPED--LSRRIEQLQQREIVLKEENSsltssarqlekarrELEQELAQYLKKIEDLNKKLKRHKAL 340
|
250
....*....|...
gi 2462539542 382 RERLYGKKIQLNR 394
Cdd:pfam05557 341 VRRLQRRVLLLTK 353
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
227-385 |
9.96e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 40.62 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 227 LKQQERRQQQSISENEKLQKLKERVEAqenklKKIRamrgqvdyskimngnlsAEIERFSAMFQEK-KQEVQtailrvdQ 305
Cdd:pfam12474 27 LEQLERQQKQQIEKLEQRQTQELRRLP-----KRIR-----------------AEQKKRLKMFRESlKQEKK-------E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 306 LSQQLEDLKKGKLNgfqsyngkltgpaavELKRLYQELQirnqlnqeQNSKLQQQKELLNKRNME-VAMMDKRISELRER 384
Cdd:pfam12474 78 LKQEVEKLPKFQRK---------------EAKRQRKEEL--------ELEQKHEELEFLQAQSEAlERELQQLQNEKRKE 134
|
.
gi 2462539542 385 L 385
Cdd:pfam12474 135 L 135
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-385 |
1.12e-03 |
|
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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 218 VAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQvdyskimngnLSAEIERFSAMFQEKKQEVQ 297
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----------AEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 298 TAILRVDQLSQQLEDLKKGklngfqsyngkltgpAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKR 377
Cdd:COG1196 376 EAEEELEELAEELLEALRA---------------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
....*...
gi 2462539542 378 ISELRERL 385
Cdd:COG1196 441 EEALEEAA 448
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
733-965 |
1.14e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 733 SLSTGTPQPQPPSESTEKEPEqdgPAAPADGSTVESLPRPLSPTKLTPIVHSPLRYQSDADLealRRKLANAPRPLKKRS 812
Cdd:PRK12323 366 GQSGGGAGPATAAAAPVAQPA---PAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPA---RRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 813 SITEPEGPGGPniqkllyqrfntlAGGMEGTPFYQPSPsqdfmgtladvdngntnANGNLEELPPAQPTAPLPAEPAPSS 892
Cdd:PRK12323 440 SARGPGGAPAP-------------APAPAAAPAAAARP-----------------AAAGPRPVAAAAAAAPARAAPAAAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462539542 893 DANDNELPSPE--PEELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAPLPPASHPPAT 965
Cdd:PRK12323 490 APADDDPPPWEelPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-398 |
1.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 191 RVELTLSELQDMAARQQQQIENQQQMLVAKEQRLHFLkqQERRQQQSISENEKLQKLKER----VEAQENkLKKIRAMRG 266
Cdd:pfam01576 212 KLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAA--LARLEEETAQKNNALKKIRELeaqiSELQED-LESERAARN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 267 QVDYSKimnGNLSAEIERF----------SAMFQE--------------------KKQEVQTAILR------VDQLSQQL 310
Cdd:pfam01576 289 KAEKQR---RDLGEELEALkteledtldtTAAQQElrskreqevtelkkaleeetRSHEAQLQEMRqkhtqaLEELTEQL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 311 EDLKKGKLN------GFQSYNGKLtgpaAVELKRLYQelqiRNQLNQEQNSKLQQQKELLNKRNMEVammDKRISELRER 384
Cdd:pfam01576 366 EQAKRNKANlekakqALESENAEL----QAELRTLQQ----AKQDSEHKRKKLEGQLQELQARLSES---ERQRAELAEK 434
|
250
....*....|....
gi 2462539542 385 LYGKKIQLNRVNGT 398
Cdd:pfam01576 435 LSKLQSELESVSSL 448
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
995-1063 |
1.38e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 41.86 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462539542 995 LLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWGAGKA 1063
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-396 |
1.46e-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: 42.74 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 191 RVELTLSELQDMAARQQQQIENQQQMLVAKEQRLHFLKQ-QERRQQQSISENEKLQKLKERVEAQENKLKKIRA------ 263
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeae 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 264 -----MRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKK---------GKLNG-FQSYNGKL 328
Cdd:TIGR02168 782 aeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERrledleeqiEELSEdIESLAAEI 861
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462539542 329 TgpaavELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRnMEVAM-----MDKRISELRERLYGKKIQLNRVN 396
Cdd:TIGR02168 862 E-----ELEELIEELESELEALLNERASLEEALALLRSE-LEELSeelreLESKRSELRRELEELREKLAQLE 928
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-364 |
1.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 128 HMMYEHLQKWGPRREEVKFFLRHEDSPTENSEQGGRQTQE--QRTQRNVINvpgEKRTENGVGNPRV---ELTLSELQDM 202
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKelMHQARTVLK---ARTEAHFNNNEEVtaaLQTGAELSHL 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 203 AARQQQQIEnqqqmlvAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQEnklkkiramRGQVDYSKIMNGNLSAEI 282
Cdd:TIGR00618 784 AAEIQFFNR-------LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE---------EEQFLSRLEEKSATLGEI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 283 ERFSAMFQEKKQEVQTAILRVDQLSQQLEDL-----KKGKLNG--FQSYNGKLTGPAAVELKRLYQELQIRNQLNQEQNS 355
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDKLnginqIKIQFDGdaLIKFLHEITLYANVRLANQSEGRFHGRYADSHVNA 927
|
....*....
gi 2462539542 356 KLQQQKELL 364
Cdd:TIGR00618 928 RKYQGLALL 936
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
716-957 |
2.09e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 42.38 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 716 VLPSGSTSPSPLPFLHGSLSTGTPQPQPPSESTEKEPEQDGPAAPADGSTveslPRPLSPTKLTPIVHSPLRYQSDADLE 795
Cdd:PRK10263 292 VLFSGNRATQPEYDEYDPLLNGAPITEPVAVAAAATTATQSWAAPVEPVT----QTPPVASVDVPPAQPTVAWQPVPGPQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 796 ALRRKLANAPRPLKKRSSITEPEGPggpniqkllyqrfntlaggmEGTPFYQPSPSQDFMGTLAdvdnGNTNANGNLEEL 875
Cdd:PRK10263 368 TGEPVIAPAPEGYPQQSQYAQPAVQ--------------------YNEPLQQPVQPQQPYYAPA----AEQPAQQPYYAP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 876 PPAQPTAPLPAEPAPSSDANDNELPSPEPEELICPQTTHQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAP 955
Cdd:PRK10263 424 APEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPAR 503
|
..
gi 2462539542 956 LP 957
Cdd:PRK10263 504 PP 505
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
219-384 |
2.45e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHFL--KQQERRQQQSISENEKLQKLKERVEAQE-----NKLKKIRAMRGQVDYSKIMN----------GNLSAE 281
Cdd:pfam02463 170 KKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKlneeridllqELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 282 IERFSAMFQE--KKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGKLtGPAAVELKRLYQELQIRNQLNQEQNSKLQ- 358
Cdd:pfam02463 250 QEEIESSKQEieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-KSELLKLERRKVDDEEKLKESEKEKKKAEk 328
|
170 180 190
....*....|....*....|....*....|
gi 2462539542 359 ----QQKELLNKRNMEVAMMDKRISELRER 384
Cdd:pfam02463 329 elkkEKEEIEELEKELKELEIKREAEEEEE 358
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
190-385 |
2.53e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 190 PRVELTLSELQD--------MAARQQQQIENQQQMLVAKEQRLHFlKQQERRQQQSISE-NEKLQKLKERVEAQENKLKK 260
Cdd:pfam07888 27 PRAELLQNRLEEclqeraelLQAQEAANRQREKEKERYKRDREQW-ERQRRELESRVAElKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 261 IRAMRGQVDYSKIMNGNLSA-------EIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGKLTGpAA 333
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAahearirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ-TE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462539542 334 VELKRLYQELQ-IRNQLNQEQNSKLQQQKEL---------LNKRNMEVAMMDKRISELRERL 385
Cdd:pfam07888 185 EELRSLSKEFQeLRNSLAQRDTQVLQLQDTIttltqklttAHRKEAENEALLEELRSLQERL 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
228-392 |
2.80e-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: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 228 KQQERRQQQSisenEKLQKLKERVEAQENKLKKIRAMRGQVdyskimngnLSAEIERFSAMFQEKKQEVQTAILRVDQLS 307
Cdd:TIGR02168 200 RQLKSLERQA----EKAERYKELKAELRELELALLVLRLEE---------LREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 308 QQLEDLKKGKLngfqsyngkltgpaavELKRLYQELQIR-NQLNQEQnSKLQQQKELLNKRNMEVAMMDKRISELRERLY 386
Cdd:TIGR02168 267 EKLEELRLEVS----------------ELEEEIEELQKElYALANEI-SRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
....*.
gi 2462539542 387 GKKIQL 392
Cdd:TIGR02168 330 SKLDEL 335
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
876-966 |
3.61e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 41.24 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 876 PPAQPTAPLPAePAPSSDANDNELPSPEPEELICPQTTHQTAEP--AEDNNNNVATVPTTEQIPSPVAEAPSPG------ 947
Cdd:PRK14951 380 TPARPEAAAPA-AAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPpaPVAAPAAAAPAAAPAAAPAAVALAPAPPaqaape 458
|
90 100
....*....|....*....|....*....
gi 2462539542 948 ----------EEQVPPAPLPPASHPPATS 966
Cdd:PRK14951 459 tvaipvrvapEPAVASAAPAPAAAPAAAR 487
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
1028-1058 |
3.77e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.79 E-value: 3.77e-03
10 20 30
....*....|....*....|....*....|.
gi 2462539542 1028 LHNAVCAGHHHIVKFLLDFGVNVNAADSDGW 1058
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGR 31
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-385 |
3.86e-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: 41.59 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 196 LSELQDmAARQQQQIENQQQMLVAKEQRLHFLKQQERRQQQSISE-----NEKLQKLKERVEAQENKLKKIRA----MRG 266
Cdd:TIGR02169 708 SQELSD-ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvKSELKELEARIEELEEDLHKLEEalndLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 267 QVDYSKIMN-GNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKkgklngfqsyngkltgpaavelkrlyQELQI 345
Cdd:TIGR02169 787 RLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI--------------------------QELQE 840
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462539542 346 RNQLNQEQNSKLQQQKELLNKR----NMEVAMMDKRISELRERL 385
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKkeelEEELEELEAALRDLESRL 884
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
531-775 |
4.21e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 41.07 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 531 PVPFSALGPTEKPgieIGKVPPPIPGVGKQLPPSYGTYPSPTPLGPgsTSSLERRKEGSLPRPSaglpsrqrptllPATG 610
Cdd:PLN03209 331 KESDAADGPKPVP---TKPVTPEAPSPPIEEEPPQPKAVVPRPLSP--YTAYEDLKPPTSPIPT------------PPSS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 611 STPQPGSSQQIQQ--RISVPPSP-TYPPAGPPAFPAGDSKPELPLTvairPFLA-DKGSRPQSPRKGPQ-----TVNSSS 681
Cdd:PLN03209 394 SPASSKSVDAVAKpaEPDVVPSPgSASNVPEVEPAQVEAKKTRPLS----PYARyEDLKPPTSPSPTAPtgvspSVSSTS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 682 IYSMYLQQATPPKNYQPAAHSALNKSVKAVYGKPVLPSGSTSPSPlpflhgsLSTGTPQPQPPSESTEKEPEQDGPAAPA 761
Cdd:PLN03209 470 SVPAVPDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSP-------AAPVGKVAPSSTNEVVKVGNSAPPTALA 542
|
250
....*....|....*
gi 2462539542 762 D-GSTVESLPRPLSP 775
Cdd:PLN03209 543 DeQHHAQPKPRPLSP 557
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
591-968 |
4.59e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 41.29 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 591 PRPSAGLPSRQRPTLLPATGSTPQPGSSQQIQQRISVPPSPTYPPAGPPAFPAGDSKPELPLTVAIRPfladkgsrPQSP 670
Cdd:pfam03154 188 PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQP--------PPPS 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 671 RKGPQTVNSSSiysmyLQQATPPKNYQPAAHSALNKSVKAVYGKPVLPSGSTS---PSPLPFLHGSLSTGTPQPQPPSES 747
Cdd:pfam03154 260 QVSPQPLPQPS-----LHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSqvpPGPSPAAPGQSQQRIHTPPSQSQL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 748 TEKEPEQDGPAAPADGSTVESLPRPLSPT---------KLTPIVHSPLRYQSDADLEAlrrklanaPRPLKKRSSITEPE 818
Cdd:pfam03154 335 QSQQPPREQPLPPAPLSMPHIKPPPTTPIpqlpnpqshKHPPHLSGPSPFQMNSNLPP--------PPALKPLSSLSTHH 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 819 GPGG--PNIQKllyqrfntlaggMEGTPFYQPSPSQDFMGTLADVDNGNTNANGNLEELPPAQPTAPLPAEPAPSSDAND 896
Cdd:pfam03154 407 PPSAhpPPLQL------------MPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPP 474
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462539542 897 NELPSPEPEELICPQTTHQtaEPAEDNNNNVATVPTTEQIPSPVA----EAPSPGEEQVPPAPLPPASHPPATSTN 968
Cdd:pfam03154 475 ITPPSGPPTSTSSAMPGIQ--PPSSASVSSSGPVPAAVSCPLPPVqikeEALDEAEEPESPPPPPRSPSPEPTVVN 548
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-394 |
4.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 221 EQRLHFLKQQERRQQQSISENEKLQKLK---ERVEAQENKLKKI---RAMRGQVDYSKI---MNG------NLSAEIERF 285
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKKYnleELEKKAEEYEKLkekLIKlkgeikSLKKELEKL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 286 SAmFQEKKQEVQTAIlrvDQLSQQLEDLKKGKLN-GFQSY---NGKLTgpaavELKRLY----------QELQIRNQLNQ 351
Cdd:PRK03918 552 EE-LKKKLAELEKKL---DELEEELAELLKELEElGFESVeelEERLK-----ELEPFYneylelkdaeKELEREEKELK 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462539542 352 EQNSKLQQQKELLNKRNMEVAMMDKRISELR--------ERLYGKKIQLNR 394
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEkkyseeeyEELREEYLELSR 673
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
1020-1057 |
5.12e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.42 E-value: 5.12e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2462539542 1020 PNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDG 1057
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225
|
|
| PilN |
COG3166 |
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures]; |
221-275 |
5.53e-03 |
|
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
Pssm-ID: 442399 [Multi-domain] Cd Length: 185 Bit Score: 39.18 E-value: 5.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2462539542 221 EQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRgqVDYSKIMN 275
Cdd:COG3166 51 QARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQSR--PPWVHLLD 103
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
401-793 |
6.13e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 401 PQSPLSTSGRVAAVGPYIQVPSAGSFPVLGDPIKPQSLSIASNAAHgrsksdghSKPRVTSSWTVSDLDVGPNYGSSRP- 479
Cdd:PHA03247 2691 TVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALP--------AAPAPPAVPAGPATPGGPARPARPPt 2762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 480 -----SASPFVNPNDGNWPTLKQNSSSSVKPVQVAGADWKDPSVEGSVkqgtvssQPVPFSALGPTEKPGieiGKVPPPI 554
Cdd:PHA03247 2763 tagppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPA---GPLPPPT 2832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 555 PGVGKQLPPSYGTYPSPTPLGPGSTSSLERRKEGSLPRPSAGLPSRQRPTLLPATGSTPQPGSSQQIQQRISVPPSPTYP 634
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQ 2912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 635 PAGPPAFPAGDSKPELPLTVAIRPFLADKGSRPQsPRKGPQTVNSSSIYSMYLQQATPPKNYQPAAHSALNKsvkavygk 714
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT-TDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA-------- 2983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 715 pvlPSGSTSPSPLPFLHGSLSTGT------------PQPQPPSESTEKEPEQDGPAAPADGSTV-------ESLPRPLSP 775
Cdd:PHA03247 2984 ---PSREAPASSTPPLTGHSLSRVsswasslalheeTDPPPVSLKQTLWPPDDTEDSDADSLFDsdsersdLEALDPLPP 3060
|
410
....*....|....*...
gi 2462539542 776 TKLTPIVHSPLRYQSDAD 793
Cdd:PHA03247 3061 EPHDPFAHEPDPATPEAG 3078
|
|
| PRK11901 |
PRK11901 |
hypothetical protein; Reviewed |
836-968 |
7.54e-03 |
|
hypothetical protein; Reviewed
Pssm-ID: 237015 [Multi-domain] Cd Length: 327 Bit Score: 39.67 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 836 LAGGMEGTPFYQPSPSQDFMGTLADVDNGNTNANGNLEELPPaqPTAPLPAEPAPSSDANDN---ELPSPEPEELicPQT 912
Cdd:PRK11901 81 LSGSSSLSSGNQSSPSAANNTSDGHDASGVKNTAPPQDISAP--PISPTPTQAAPPQTPNGQqriELPGNISDAL--SQQ 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462539542 913 THQTAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGEEQVPPAPL-------PPASHPPATSTN 968
Cdd:PRK11901 157 QGQVNAASQNAQGNTSTLPTAPATVAPSKGAKVPATAETHPTPPqkpatkkPAVNHHKTATVA 219
|
|
| DamX |
COG3266 |
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ... |
870-980 |
7.99e-03 |
|
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442497 [Multi-domain] Cd Length: 455 Bit Score: 40.22 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 870 GNLEELPPAQPTAPLPAEPAPSSDANDNELPSPEPEELICPQTTHQ-TAEPAEDNNNNVATVPTTEQIPSPVAEAPSPGE 948
Cdd:COG3266 252 GSALKAPSQASSASAPATTSLGEQQEVSLPPAVAAQPAAAAAAQPSaVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTE 331
|
90 100 110
....*....|....*....|....*....|..
gi 2462539542 949 EQVPPAPLPPASHPPATSTNKRTNLKKPNSER 980
Cdd:COG3266 332 TAAPAAPAPEAAAAAAAPAAPAVAKKLAADEQ 363
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
219-385 |
8.84e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 219 AKEQRLHF---LKQQERRQQQSISENEKLQklkERVEAQENKLKKIRAMRGQVDYSKI--------MNGNLSAEIERFSA 287
Cdd:pfam01576 17 VKERQQKAeseLKELEKKHQQLCEEKNALQ---EQLQAETELCAEAEEMRARLAARKQeleeilheLESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462539542 288 MFQEKKqEVQTAILrvdQLSQQL--EDLKKGKLNgfqsyNGKLTGPAavELKRLYQELQIRnqlnQEQNSKLQQQKELLN 365
Cdd:pfam01576 94 LQNEKK-KMQQHIQ---DLEEQLdeEEAARQKLQ-----LEKVTTEA--KIKKLEEDILLL----EDQNSKLSKERKLLE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462539542 366 KRNME-----------VAMMDK-------RISELRERL 385
Cdd:pfam01576 159 ERISEftsnlaeeeekAKSLSKlknkheaMISDLEERL 196
|
|
| |
