|
Name |
Accession |
Description |
Interval |
E-value |
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
1.76e-57 |
|
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
Pssm-ID: 461885 [Multi-domain] Cd Length: 195 Bit Score: 194.80 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568914310 434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
|
|
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
622-806 |
1.57e-49 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 179.00 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180
....*....|....*....|....*
gi 568914310 782 ERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKP 181
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
623-806 |
3.75e-42 |
|
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.
Pssm-ID: 214697 [Multi-domain] Cd Length: 392 Bit Score: 158.67 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180
....*....|....*....|....*.
gi 568914310 781 IERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKP 181
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
23-275 |
3.68e-22 |
|
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.
Pssm-ID: 461886 Cd Length: 188 Bit Score: 94.69 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 568914310 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-486 |
2.47e-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: 41.58 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 568914310 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
2.65e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 568914310 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
1.76e-57 |
|
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
Pssm-ID: 461885 [Multi-domain] Cd Length: 195 Bit Score: 194.80 E-value: 1.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568914310 434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
|
|
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
622-806 |
1.57e-49 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 179.00 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180
....*....|....*....|....*
gi 568914310 782 ERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKP 181
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
623-806 |
3.75e-42 |
|
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.
Pssm-ID: 214697 [Multi-domain] Cd Length: 392 Bit Score: 158.67 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180
....*....|....*....|....*.
gi 568914310 781 IERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKP 181
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
23-275 |
3.68e-22 |
|
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.
Pssm-ID: 461886 Cd Length: 188 Bit Score: 94.69 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 568914310 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
355-478 |
1.81e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 43.35 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 355 KLKHTESD--KLQVQIQAYLDNVFDvgalledaetKNAAlERvEELEENISHLSEKLQDTENeamsKIVELEKQLMQRNK 432
Cdd:pfam15619 89 KLKEKEAEllRLRDQLKRLEKLSED----------KNLA-ER-EELQKKLEQLEAKLEDKDE----KIQDLERKLELENK 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568914310 433 ELDvvREIYKdANTQVHTLRKMVKEKEEAIQRqstLEKKIHELEKQ 478
Cdd:pfam15619 153 SFR--RQLAA-EKKKHKEAQEEVKILQEEIER---LQQKLKEKERE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
349-478 |
5.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHTESDKLQVQIQAYLDNVF---------DVGALLEDAETKNAALERVEELEENI-SHLSEKLQD----TEN 414
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLaeagvedeeELRAALEQAEEYQELKEELEELEEQLeELLGELEELlealDEE 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914310 415 EAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKmVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-478 |
8.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 364 LQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTEnEAMSKIVELEKQLMQRNKELDVVREIYKD 443
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASSDDLAALEEQ 693
|
90 100 110
....*....|....*....|....*....|....*
gi 568914310 444 ANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
353-478 |
1.29e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 353 LDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETK-----NAALERVEELEENISHLSEKLQDTENEamskiVELEKQL 427
Cdd:pfam09787 49 LEELRQ-ERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaESSREQLQELEEQLATERSARREAEAE-----LERLQEE 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914310 428 MQRNKElDVVREI------YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHEL-----EKQ 478
Cdd:pfam09787 123 LRYLEE-ELRRSKatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLtetliQKQ 183
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
354-485 |
1.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 354 DKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdtenEAMSKIVELEKQLMQRNKE 433
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568914310 434 LDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQK 485
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
349-496 |
1.79e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHTESDKLQvqiQAYLDNVFDVGALLEDAETKNAALE-RVEELEENISHLSEKLQDTENEAMSKIVELEKQL 427
Cdd:COG2433 378 IEEALEELIEKELPEEE---PEAEREKEHEERELTEEEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914310 428 MQRNKELDVVREIYKDANTqVHTLRKMVKEKEEAIQRqstLEKKIHELEKqgTIKIQKKGDGdIAILPV 496
Cdd:COG2433 455 SEERREIRKDREISRLDRE-IERLERELEEERERIEE---LKRKLERLKE--LWKLEHSGEL-VPVKVV 516
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
385-478 |
2.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 385 AETKNAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAI-- 462
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELes 105
|
90
....*....|....*...
gi 568914310 463 --QRQSTLEKKIHELEKQ 478
Cdd:COG4372 106 lqEEAEELQEELEELQKE 123
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
290-475 |
2.26e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 290 FKEVCGEKQRFEKLMEHFRNE--------DNNIDFMVASMQFINIVVHSVE-DMNFRVHLQYEFTKLGLDEYLDKL--KH 358
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREEtrqvymdlNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEEYKKEIndKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 359 TESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELE-ENISHLSEKlqdteNEAMSKIVELEKQLMQRNkeLDVV 437
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdENLKELIEK-----KDHLTKELEDIKMSLQRS--MSTQ 312
|
170 180 190
....*....|....*....|....*....|....*...
gi 568914310 438 REIYKDANTQVHTLRKMVKEKEEAIQrQSTLEKKIHEL 475
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQME-ELNKAKAAHSF 349
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-486 |
2.47e-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: 41.58 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 568914310 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
2.65e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 568914310 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
353-452 |
3.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 353 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 421
Cdd:PRK11281 45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124
|
90 100 110
....*....|....*....|....*....|.
gi 568914310 422 ELEKQLMQRNKELDVVREIYKDANTQVHTLR 452
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
378-478 |
4.20e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 378 VGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLmQRNKELDVVREIYKDANTQVHTLRKMVK 456
Cdd:pfam15905 175 VMAKQEGMEGKlQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLL-EYITELSCVSEQVEKYKLDIAQLEELLK 253
|
90 100
....*....|....*....|...
gi 568914310 457 EKEEAIQR-QSTLEKKIHELEKQ 478
Cdd:pfam15905 254 EKNDEIESlKQSLEEKEQELSKQ 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-478 |
4.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 380 ALLEDAETKNAALERVEELEENISHLSEKLQDTEneamSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRkmvKEKE 459
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALE---AELA 86
|
90
....*....|....*....
gi 568914310 460 EAIQRQSTLEKKIHELEKQ 478
Cdd:COG4942 87 ELEKEIAELRAELEAQKEE 105
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
349-478 |
5.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETknaaleRVEELEENISHLSEKLQDTEneamSKIVELEKQLM 428
Cdd:COG1579 15 LDSELDRLEH-RLKELPAELAELEDELAALEARLEAAKT------ELEDLEKEIKRLELEIEEVE----ARIKKYEEQLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914310 429 Q--RNKELDVV-REI-------------YKDANTQVHTLRKMVKEKEEAI-QRQSTLEKKIHELEKQ 478
Cdd:COG1579 84 NvrNNKEYEALqKEIeslkrrisdledeILELMERIEELEEELAELEAELaELEAELEEKKAELDEE 150
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-478 |
7.15e-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: 40.04 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 384 DAETKNAALERVEELEENISHLsEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQ 463
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90
....*....|....*....
gi 568914310 464 ----RQSTLEKKIHELEKQ 478
Cdd:TIGR02168 744 qleeRIAQLSKELTELEAE 762
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
357-478 |
7.84e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 357 KHTESDKLQVQIQayldnvfdvgallEDAETKNAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELDV 436
Cdd:TIGR04523 122 LEVELNKLEKQKK-------------ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ----KEELENELNLLEKEKLN 184
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568914310 437 VREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
|
| DUF2312 |
pfam10073 |
Uncharacterized protein conserved in bacteria (DUF2312); Members of this family of ... |
393-444 |
8.03e-03 |
|
Uncharacterized protein conserved in bacteria (DUF2312); Members of this family of hypothetical bacterial proteins have no known function. Structural modelling suggests this domain may bind nucleic acids.
Pssm-ID: 431032 Cd Length: 72 Bit Score: 35.62 E-value: 8.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568914310 393 ERVEELEENISHLSEKLQDTENEA---------MSKIVELEKQLMQRNKELDVVREIYKDA 444
Cdd:pfam10073 10 ERIERLEEEKKAIAEDIKDVYAEAkgrgfdtkvMRKIVKLRKMDKDERQEQEALLELYKAA 70
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
367-478 |
9.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdTEN-----EAMSKIVELEKQLMQRNKE-LDVVREI 440
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY--TPNhpdviALRAQIAALRAQLQQEAQRiLASLEAE 321
|
90 100 110
....*....|....*....|....*....|....*...
gi 568914310 441 YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
386-462 |
9.41e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 386 ETKNAALERVEELEENISHLSEKLQD------TENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK- 458
Cdd:COG0542 433 EQDEASFERLAELRDELAELEEELEAlkarweAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEv 512
|
....*
gi 568914310 459 -EEAI 462
Cdd:COG0542 513 tEEDI 517
|
|
|