|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
18-162 |
2.34e-49 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 173.56 E-value: 2.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 18 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG----DKEKKPVCTNPLSI 92
Cdd:pfam09727 2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdEDVYEAMYEKPLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 136
Cdd:pfam09727 82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
|
170 180
....*....|....*....|....*.
gi 1390010537 137 KLAARLEEERGKNKQVVLMLVKECKQ 162
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
680-952 |
3.49e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.59 E-value: 3.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 680 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNG 759
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:COG0666 121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 840 SLKLLMyhripAHGnsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGG 919
Cdd:COG0666 201 IVKLLL-----EAG-------------------------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
|
250 260 270
....*....|....*....|....*....|...
gi 1390010537 920 LEPERRDKCNRTVHDVATDDCKHLLENLNALKI 952
Cdd:COG0666 244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
694-936 |
1.49e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 137.78 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 774 CVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHG 853
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-----EAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 854 nsfneeesessvfdldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVH 933
Cdd:COG0666 177 -------------------------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTAL 223
|
...
gi 1390010537 934 DVA 936
Cdd:COG0666 224 DLA 226
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
730-817 |
1.27e-24 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 99.42 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 730 LYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYdANINhAADGGQTPLYLACKNGNKECIK 809
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
....*...
gi 1390010537 810 LLLEAGTN 817
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
707-946 |
6.53e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 100.80 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 707 LLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANIN 786
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 787 HAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMyhripAHGnsfneeesessvf 866
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAG------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 867 dldggeespegiskpvvpADlINHANREGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHDVA-----TDDCK 941
Cdd:COG0666 144 ------------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVK 203
|
....*
gi 1390010537 942 HLLEN 946
Cdd:COG0666 204 LLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
696-786 |
1.07e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 696 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSaEAQVNAADkNGFTPLCAAAAQGHFECV 775
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 1390010537 776 ELLISYDANIN 786
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
763-849 |
1.11e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSvkTTDGWTPVHAAVDTGNVDSLK 842
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
|
....*..
gi 1390010537 843 LLMYHRI 849
Cdd:pfam12796 79 LLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
703-849 |
9.83e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.64 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 703 GNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKngftplcaaaaqghfecVELLIS 780
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 781 YDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRI 849
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
714-833 |
1.38e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 81.16 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 714 EEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ 793
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1390010537 794 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 833
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
694-848 |
5.87e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.24 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 774 CVELLISYDANINHAADGGQTPLYLACKNgNKECIKLLLeagTNRSVKTTD--GWTPVHAAVDTG-NVDSLKLLMYHR 848
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI---NNASINDQDidGSTPLHHAINPPcDIDIIDILLYHK 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
695-844 |
6.74e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 695 LLQQAAAQGNVTLLSM-LLNEEGLDINYSCEDGHSALYSAAKNGHTDC---VRLLLSAEAQVNAADKNGFTPL-CAAAAQ 769
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 770 GHFECVELLISYDANINHAADGGQTPL--YLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD--SLKLL 844
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
699-848 |
1.97e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 77.34 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 699 AAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 779 ISYDANINHAA-DGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 848
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
711-845 |
7.01e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 711 LLNEEGLDINYSCED-GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAA 789
Cdd:PHA02878 152 LLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 790 DGGQTPLYLA---CKngNKECIKLLLEAGTNRSVKTT-DGWTPVHAAVDTGnvDSLKLLM 845
Cdd:PHA02878 232 KCGNTPLHISvgyCK--DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLL 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
796-926 |
7.05e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 796 LYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHripahgnsfneeesessvfdldggeesp 875
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 876 egiskpvVPADLINHanreGWTAAHIAASKGFKNCLEILCRHgGLEPERRD 926
Cdd:pfam12796 53 -------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
699-845 |
4.63e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 74.52 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 699 AAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 779 ISYdANINHAADGGQTpLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLM 845
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-253 |
1.30e-12 |
|
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: 73.18 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 19 SKSELRMLLSVMEGELEARDLVIEALRAR--RKEVFIQERYGRFN--LNDPFLALQRDYEAGAGDKEKkpvctnplsiLE 94
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIAS----------LE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 95 AVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 EDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQM-------EKQLSEFDTERE--------------QLRAKLNRE 230
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDrlqEELQRLSEELADLnaaiagiEAKINELEEEKEdkaleikkqewkleQLAADLSKY 467
|
250 260
....*....|....*....|...
gi 1390010537 231 EAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQR 490
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
704-847 |
1.38e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.22 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 704 NVTLLSMLL-----NEEGLDINYSCEDGHSALYSaaknghTDCVRLLLSAEAQVNAADKN-GFTPLCAAAAQGHFECVEL 777
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 778 LISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDT-GNVDSLKLLMYH 847
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
726-779 |
1.44e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 63.83 E-value: 1.44e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 726 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLI 779
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-246 |
1.50e-12 |
|
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: 69.18 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGK------NKQVVLMLvKECKQLSGKVIEEAQKL 174
Cdd:COG1579 34 AELEDELAALEARLEAAKTEledlEKEIKRLELEIEEVEARIKKYEEQlgnvrnNKEYEALQ-KEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAHTT---DLKEEIDKMRK 246
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REELAAKippELLALYERIRK 185
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
694-847 |
3.18e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.76 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLNEeGLDINYSCEDGHSALYSAAKNGHTDCVRLL-----------------------LSAEA 750
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 751 QVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 830
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170
....*....|....*..
gi 1390010537 831 AAVDTGNVDSLKLLMYH 847
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-253 |
3.69e-12 |
|
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: 71.63 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 189 NELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168 347 EELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
761-812 |
4.09e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 62.29 E-value: 4.09e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 761 TPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 812
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
105-279 |
5.15e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEE-----ERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 179
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 180 KLEEEKKKTNELEEELSAEKRRSTEMEAQM-------EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180
....*....|....*....|....*..
gi 1390010537 253 rgsDSKPSLSLPRKTKDRRLVSISVGT 279
Cdd:COG4717 234 ---NELEAAALEERLKEARLLLLIAAA 257
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
101-253 |
7.02e-12 |
|
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: 68.79 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknKQVVLMLVKECKQLSGKVIE---EAQKLED 176
Cdd:pfam13868 80 EQIEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKElekEEEREED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 177 V-----MAKLEEEKKKTNELEEELSAEK-RRSTEMEAQMEKQLSEFDtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:pfam13868 155 ErileyLKEKAEREEEREAEREEIEEEKeREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQERKERQKEREEAEKKARQ 233
|
...
gi 1390010537 251 LKR 253
Cdd:pfam13868 234 RQE 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-254 |
1.22e-11 |
|
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: 70.10 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 20 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGAGDKEKKPvctnplSILEAV 96
Cdd:TIGR02169 673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK------ERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAARLEEERGKNKQVVLMLVKE-CKQLSGKVIEEA 171
Cdd:TIGR02169 743 EEDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEeVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
....*.
gi 1390010537 249 EQLKRG 254
Cdd:TIGR02169 899 RELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-304 |
1.76e-11 |
|
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: 69.32 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGK---NKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnREEAhtTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAEL--TLLNEEAANLRERLESLER 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 254 GSDSKpslslprKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKL 304
Cdd:TIGR02168 832 RIAAT-------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-253 |
2.15e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekkpvctnpLSILEAVMAHCK 101
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE-----------LARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 102 KMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDV 177
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEeleeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAKL---EEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:COG1196 389 LEALraaAELAAQLEELEEAEEALLERLERLEEELeelEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
..
gi 1390010537 252 KR 253
Cdd:COG1196 469 LE 470
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
680-845 |
3.46e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 67.32 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 680 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYscEDGHSALYSAAKNGHTDCVRLLLSAEAQVNA 754
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 755 ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDG-WTPVHAAV 833
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|..
gi 1390010537 834 DTGNVDSLKLLM 845
Cdd:PHA02875 211 ENNKIDIVRLFI 222
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
694-796 |
3.49e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.13 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFE 773
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
|
90 100
....*....|....*....|...
gi 1390010537 774 CVELLISYDANINHAADGGQTPL 796
Cdd:COG0666 267 IVKLLLLALLLLAAALLDLLTLL 289
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-271 |
3.52e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvvLMLVKECKQLSGKVIEEAQKLEDVMAK 180
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE---AEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 181 LEEEKKKTNELEEELSAEKRRSTEME--AQMEKQLSEFDTEREQLR----AKLNREEAHTTD-LKEEIDKMRKMIEQLKR 253
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADeAKKKAEEAKKAEEAKKK 1465
|
170
....*....|....*...
gi 1390010537 254 GSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAK 1483
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
92-253 |
1.22e-10 |
|
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: 64.94 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 92 ILEAVMAHCKKMQ------ERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLAARLE---EERGKNKQVVLMLVKECKQ 162
Cdd:pfam13868 23 ERDAQIAEKKRIKaeekeeERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEeqiEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 163 LSGKVIEEAQkLEDVMAKLEEEKKKTNELEE--ELSAEKRRSTEMEAQMEK----QLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:pfam13868 102 QMDEIVERIQ-EEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEEReedeRILEYLKEKAEREEEREAEREEIEE 180
|
170
....*....|....*...
gi 1390010537 237 LKE-EIDKMRKMIEQLKR 253
Cdd:pfam13868 181 EKErEIARLRAQQEKAQD 198
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
118-253 |
1.39e-10 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 60.29 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKLQLQALEQEHKKLAARLEeergknkqVVLMLVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSA 197
Cdd:pfam18595 1 SSTLAEEKEELAELERKARELQAKID--------ALQVVEKDLR----SCIKLLEEIEAELAKLEEAKKKLKELRDALEE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 198 EKRRSTEMEA---QMEKQLsefdterEQLRAKLNREEAHTtdlKEEIDKMRKMIEQLKR 253
Cdd:pfam18595 69 KEIELRELERreeRLQRQL-------ENAQEKLERLREQA---EEKREAAQARLEELRE 117
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
90-259 |
1.65e-10 |
|
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: 64.79 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQA-LEQEHKKLAARLEE--ERGKNKQVVLML---------- 156
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 157 --------VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:COG4942 137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
170 180 190
....*....|....*....|....*....|.
gi 1390010537 229 REEAHTTDLKEEIDKMRKMIEQLKRGSDSKP 259
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
712-847 |
1.67e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.07 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 712 LNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGH-----FECVELLISYDANIN 786
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 787 HAADGGQTPLYLA--CKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDS--LKLLMYH 847
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDK 165
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
120-313 |
1.91e-10 |
|
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: 65.90 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 120 KLEMEKLQLQALEQEHKKlaarleEERGKNKQVVLMLVKeckqlsgkVIEEAQKLEDVMAKLEEEKKKTNELEEElsaEK 199
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKK------EINDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 200 RRSTEMEAQMEKQlSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGT 279
Cdd:pfam05483 279 LQDENLKELIEKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190
....*....|....*....|....*....|....
gi 1390010537 280 EGTVTRSVACQTDLVTENADHMKKLPLTMPVKPS 313
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
119-258 |
2.24e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 119 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAE 198
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 199 KR---RSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:COG4372 86 NEqlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-252 |
2.60e-10 |
|
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: 65.47 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 21 SELRMLLSVMEGELEARDLVIEAL-RARRKEVFIQErygrfNLNDPFLALQRDYEAgagDKEKkpvctnplsiLEAVMAH 99
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLeQEEEKLKERLE-----ELEEDLSSLEQEIEN---VKSE----------LKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 100 CKKMQERMSAQLAAAESRQKKLEMEKLQ-----LQALEQEHKKLAARLEEERGKNKQVVL---MLVKECKQLSGKVIEEA 171
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPeiqaeLSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELsAEKRRStemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEEL-EELEAA---LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
.
gi 1390010537 252 K 252
Cdd:TIGR02169 923 K 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-253 |
4.78e-10 |
|
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: 64.70 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 12 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAGDKEKKpvct 87
Cdd:TIGR02169 167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYELLKEKE---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 88 nplsILEavmahckKMQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAARLEEERGKNKQVVLMLVKE 159
Cdd:TIGR02169 234 ----ALE-------RQKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 160 CKQLSGKVIEEAQKLEDV---MAKLEEEKKKT----NELEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:TIGR02169 303 IASLERSIAEKERELEDAeerLAKLEAEIDKLlaeiEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260
....*....|....*....|.
gi 1390010537 233 HTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKR 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-256 |
9.51e-10 |
|
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: 63.92 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEA-----RDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAgdkekkpvctnpLSILEAV 96
Cdd:TIGR02168 695 ELEKALAELRKELEEleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMQERMSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSGKVIEEAQ 172
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQieqlKEELKALREALDELRAELTLLNEE----AANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLEDvmakLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:TIGR02168 839 RLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
....
gi 1390010537 253 RGSD 256
Cdd:TIGR02168 915 RELE 918
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
129-254 |
9.75e-10 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 63.34 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 129 QALE-QEHKKLAARLEEERGKNKQVVLML---VKECKQLSGKViEEAQKL-EDVMAKLEEEKKKTNELEEELSaEKRRST 203
Cdd:COG2433 380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQV-ERLEAEvEELEAELEEKDERIERLERELS-EARSEE 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 204 EMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
694-756 |
1.03e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 1.03e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLNEEGLDInysCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAD 756
Cdd:pfam12796 32 TALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
92-250 |
1.06e-09 |
|
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: 62.99 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 92 ILEAVMAHCkkMQER---MSAQLAAAESRQKKLEMEKLQLQALEQEHKKL---AARLEEERGKNKQVVLMLVKECKQLSG 165
Cdd:pfam07888 31 LLQNRLEEC--LQERaelLQAQEAANRQREKEKERYKRDREQWERQRRELesrVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 166 KVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK----------QLSEFDTEREQLRAKLNREEAHTT 235
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEELR 188
|
170
....*....|....*
gi 1390010537 236 DLKEEIDKMRKMIEQ 250
Cdd:pfam07888 189 SLSKEFQELRNSLAQ 203
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
333-700 |
1.14e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.80 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 333 MARPGIDRQASYGDLIGASVPAFP----PPsankiEENGPST-GSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPm 407
Cdd:PHA03247 2455 FARTILGAPFSLSLLLGELFPGAPvyrrPA-----EARFPFAaGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEP- 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 408 hslhspcantsLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVS-PTSRdnlVAKQLARNTVTQALSRFTSP-Q 485
Cdd:PHA03247 2529 -----------VHPRMLTWIRGLEELASDDAGDPPPPLPPAAPPAAPDRSvPPPR---PAPRPSEPAVTSRARRPDAPpQ 2594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 486 AGAPSRPGVPPTGDVGTHPPV----GRTSLKTHGVARVDRGNpppippKKPGLSQTPSPPHPQLKVIIDSSRASNTgAKV 561
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSplppDTHAPDPPPPSPSPAAN------EPDPHPPPTVPPPERPRDDPAPGRVSRP-RRA 2667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 562 DNKTVASTPSSLPQGNR-------VINEENL----PKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAATPGLNQ 630
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrraarptVGSLTSLadppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG 2747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 631 PAC--SDSSLVIPTTIAFCSSINPVSASSCRP----------GASDSLLVTASGWSPSLTPLLMSG---------GPAPL 689
Cdd:PHA03247 2748 PATpgGPARPARPPTTAGPPAPAPPAAPAAGPprrltrpavaSLSESRESLPSPWDPADPPAAVLApaaalppaaSPAGP 2827
|
410
....*....|.
gi 1390010537 690 AGRPTLLQQAA 700
Cdd:PHA03247 2828 LPPPTSAQPTA 2838
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
20-249 |
1.37e-09 |
|
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: 63.27 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 20 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGAGDKEKkpvctnplsiLEAVM-- 97
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKLQ----------LEKVTte 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 98 AHCKKMQER--MSAQLAAAESRQKKL--------------EMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEC 160
Cdd:pfam01576 131 AKIKKLEEDilLLEDQNSKLSKERKLleeriseftsnlaeEEEKAKsLSKLKNKHEAMISDLEERLKKEEKGRQELEKAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 161 KQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ----------MEKQLSEFDTEREQLRAKLNRE 230
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQknnalkkireLEAQISELQEDLESERAARNKA 290
|
250
....*....|....*....
gi 1390010537 231 EAHTTDLKEEIDKMRKMIE 249
Cdd:pfam01576 291 EKQRRDLGEELEALKTELE 309
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
93-253 |
1.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESR--QKKLEMEKLQ-----LQALEQEHKKLAARLE-------EERGKNKQVVLMLVK 158
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAEleELRLELEELEleleeAQAEEYELLAELARLEqdiarleERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 159 ECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLK 238
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170
....*....|....*
gi 1390010537 239 EEIDKMRKMIEQLKR 253
Cdd:COG1196 404 ELEEAEEALLERLER 418
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-253 |
1.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 33 ELEARDLvieALRARRKEVFIQERYgrfNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHCKKMQERMSAQLA 112
Cdd:TIGR02168 221 ELRELEL---ALLVLRLEELREELE---ELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 113 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEaqKLEDVMAKLEEEKKKTNELE 192
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-----KLDELAEELAELEE--KLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 193 EELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-303 |
1.60e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKefdVDTLSKSE-LRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDK-EKKPV 85
Cdd:PTZ00121 1544 EKKK---ADELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaEEAKI 1620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 86 CTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL---QLQALEQEHKKLA--ARLEEERGKNKQVVLML---- 156
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKeaee 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 157 VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEM--EAQMEKQLSEFDTEREQLRAKLNREEAHT 234
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 235 tdLKEEIDKmrkmieqlkrgSDSKPSLSLPRKTKDRR---------------LVSISVGTEGTVTRSVACQTDLVTENAD 299
Cdd:PTZ00121 1781 --IEEELDE-----------EDEKRRMEVDKKIKDIFdnfaniieggkegnlVINDSKEMEDSAIKEVADSKNMQLEEAD 1847
|
....
gi 1390010537 300 HMKK 303
Cdd:PTZ00121 1848 AFEK 1851
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-253 |
1.73e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKkpvc 86
Cdd:PRK03918 197 EKEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 87 tnplsiLEAVMAHCKKMQERMSAQLAAAESRQKklEMEKLQLQALEQEhkklaaRLEEERGKNKQVVLMLVKECKQLSgk 166
Cdd:PRK03918 257 ------LEEKIRELEERIEELKKEIEELEEKVK--ELKELKEKAEEYI------KLSEFYEEYLDELREIEKRLSRLE-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 167 viEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEaqmekqlsEFDTEREQLRAKLNREEAHTTDLK-EEIDKMR 245
Cdd:PRK03918 321 --EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTgLTPEKLE 390
|
....*...
gi 1390010537 246 KMIEQLKR 253
Cdd:PRK03918 391 KELEELEK 398
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
22-253 |
2.13e-09 |
|
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: 61.09 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGAGDKEKKpvctnplsILEAVMAHCK 101
Cdd:pfam13868 99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKELEKEEERE--------EDERILEYLK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 102 KMQERMsaqlAAAESRQKKLEMEKlqlqalEQEHKKLAARLEEERGKNKQVVLMLVKeckqlsgKVIEEAQKLEDvmAKL 181
Cdd:pfam13868 163 EKAERE----EEREAEREEIEEEK------EREIARLRAQQEKAQDEKAERDELRAK-------LYQEEQERKER--QKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 182 EEEKKKTNELEEELS-------AEKRRSTEMEAQMEKQLSE-------FDTEREQLRAKLNRE--EAHTTDLKEEIDKMR 245
Cdd:pfam13868 224 REEAEKKARQRQELQqareeqiELKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAEKRRMkrLEHRRELEKQIEERE 303
|
....*...
gi 1390010537 246 KMIEQLKR 253
Cdd:pfam13868 304 EQRAAERE 311
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-252 |
2.45e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 10 KKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEkkpvcTNP 89
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEA-----EEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviE 169
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----E 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 170 EAQKLEDVMAKLEEEKkktNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKlnreEAHTTDLKEEIDKMRKMIE 249
Cdd:TIGR02168 853 DIESLAAEIEELEELI---EELESELEALLNERASLEEALALLRSELEELSEELREL----ESKRSELRRELEELREKLA 925
|
...
gi 1390010537 250 QLK 252
Cdd:TIGR02168 926 QLE 928
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-253 |
3.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 184 EKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-252 |
5.80e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 41 IEALRARRKEVF-----IQERYGrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI--LEAVMAHCKKMQERMSAQLAA 113
Cdd:PRK03918 393 LEELEKAKEEIEeeiskITARIG--ELKKEIKELKKAIEELKKAKGKCPVCGRELTEehRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 114 AESRQKKLEMEKLQLQ-ALEQE-----HKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKK 187
Cdd:PRK03918 471 IEEKERKLRKELRELEkVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 188 TNELEEELSA--EKRRSTEME-AQMEKQLSEFDTE----------------REQLRAK-----LNREEAHTTDLKEEIDK 243
Cdd:PRK03918 551 LEELKKKLAEleKKLDELEEElAELLKELEELGFEsveeleerlkelepfyNEYLELKdaekeLEREEKELKKLEEELDK 630
|
....*....
gi 1390010537 244 MRKMIEQLK 252
Cdd:PRK03918 631 AFEELAETE 639
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
703-845 |
8.61e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.98 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 703 GNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYD 782
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 783 AN-------------INHAADGG----------QTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVD 839
Cdd:PHA02874 92 VDtsilpipciekdmIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
....*.
gi 1390010537 840 SLKLLM 845
Cdd:PHA02874 172 IIKLLL 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-252 |
9.00e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 20 KSELRMLLSVMEGELEArdlviEALRARRKEVFIQE-RYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSILEAVMA 98
Cdd:TIGR02168 241 LEELQEELKEAEEELEE-----LTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 99 HCKKMQERMSAQLAAAESR-----------QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV----------VLMLV 157
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELeeqletlrskVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 158 KECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME-AQMEKQLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*.
gi 1390010537 237 LKEEIDKMRKMIEQLK 252
Cdd:TIGR02168 473 AEQALDAAERELAQLQ 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
109-246 |
1.06e-08 |
|
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: 57.63 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEekKKT 188
Cdd:COG1579 17 SELDRLEHRLKELPAE---LAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQLGN--VRN 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 189 NE----LEEELSAEKRRstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 246
Cdd:COG1579 88 NKeyeaLQKEIESLKRR----ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
694-746 |
1.18e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.18e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLL 746
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
349-718 |
1.29e-08 |
|
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: 60.17 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 349 GASVPAFPPPSankieenGPSTGSTPDPTSSTPPLPSNAAPPTAQTPgiAPQNSQAPPMHSLHSpcaNTSLHPglnPRIQ 428
Cdd:pfam03154 179 GAASPPSPPPP-------GTTQAATAGPTPSAPSVPPQGSPATSQPP--NQTQSTAAPHTLIQQ---TPTLHP---QRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 429 AARFRFQGnandpdqngnTTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRftSPQAGAPSRP--------GVPPTGDV 500
Cdd:pfam03154 244 SPHPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPH--SLQTGPSHMQhpvppqpfPLTPQSSQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 501 GTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIID-----------SSRASNTGAKVDNKTVAST 569
Cdd:pfam03154 307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKpppttpipqlpNPQSHKHPPHLSGPSPFQM 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 570 PSSLPQGNRVINEENLPKSSSPQLPPKPsidLTVAPAGcavsalatSQVGAWPAATPGLNQ-PACSDSSLVIPTTIAFCS 648
Cdd:pfam03154 387 NSNLPPPPALKPLSSLSTHHPPSAHPPP---LQLMPQS--------QQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQ 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 649 --SINPVSASSCRPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 718
Cdd:pfam03154 456 vpSQSPFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
118-245 |
1.39e-08 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 54.54 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKlQLQALEQEHKKLAARLEEERGKnkqvVLMLVKECKQLSgkviEEAQKLEdvmakleeekKKTNELEEELsA 197
Cdd:pfam20492 6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLE----------QKRQEAEEEK-E 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 198 EKRRSTEMEA----QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam20492 66 RLEESAEMEAeekeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAR 117
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
113-252 |
1.41e-08 |
|
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: 57.24 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 113 AAESRQKKLemekLQLQALEQEhkklAARLEEERGKnkqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELE 192
Cdd:COG1579 1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 193 EELSAEKRRSTEMEAQM-----EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG1579 66 LEIEEVEARIKKYEEQLgnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
763-852 |
1.71e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 842
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|
gi 1390010537 843 LLMYHRIPAH 852
Cdd:PTZ00322 166 LLSRHSQCHF 175
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-271 |
1.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVMA 179
Cdd:PTZ00121 1336 KKAEEaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK----KKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 180 KLEEEKKKTNELEEElSAEKRRSTEMEAQME--KQLSEFDTEREQLR-----------------AKLNREEAHTTD-LKE 239
Cdd:PTZ00121 1412 KAAAAKKKADEAKKK-AEEKKKADEAKKKAEeaKKADEAKKKAEEAKkaeeakkkaeeakkadeAKKKAEEAKKADeAKK 1490
|
170 180 190
....*....|....*....|....*....|..
gi 1390010537 240 EIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-266 |
2.03e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAAR-------LEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 172
Cdd:PTZ00121 1540 KKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLEDVMAKLEEEKKKTNEL-----EEELSAEKRRSTEMEAQMEKqlsefdterEQLRAKLNREEAHTTDLKEEIDKMRKM 247
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKA---------AEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
170
....*....|....*....
gi 1390010537 248 IEQLKRGSDSKPSLSLPRK 266
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKK 1709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-380 |
2.70e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---R-LEEERGKNKQV--VLMLVKECKQLSGKVIEEAQKL 174
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKkAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 EDVMAKLEEEKKKTNELEEELSAEKRRSTEM------EAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeedEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENK 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 246 KMIEQLKRGS--DSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVKPST------GSP 317
Cdd:PTZ00121 1730 IKAEEAKKEAeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIkdifdnFAN 1809
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 318 LVSANAKGS--VCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSST 380
Cdd:PTZ00121 1810 IIEGGKEGNlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
92-260 |
2.75e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 92 ILEAVMAHCKKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVLMLVKE 159
Cdd:COG4913 253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAeleRLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 160 CKQLSGKVIEEAQK--------LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE 231
Cdd:COG4913 332 IRGNGGDRLEQLEReierlereLEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180
....*....|....*....|....*....
gi 1390010537 232 AHTTDLKEEIDKMRKMIEQLKRGSDSKPS 260
Cdd:COG4913 412 AALRDLRRELRELEAEIASLERRKSNIPA 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
31-252 |
3.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 31 EGELEARDLVIEALRARRKEVF-----------IQERYGRFNLNDpflaLQRDYEAGAGDKEKkpvctnpLSILEAVMAH 99
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIklkelaeqlkeLEEKLKKYNLEE----LEKKAEEYEKLKEK-------LIKLKGEIKS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 100 CKKMQERmsaqLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE---------- 169
Cdd:PRK03918 544 LKKELEK----LEELKKKLAELEKK---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekeler 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 170 -------EAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEME--------AQMEKQLSEFDTEREQLRAKLNREEAHT 234
Cdd:PRK03918 617 eekelkkLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelreeyLELSRELAGLRAELEELEKRREEIKKTL 696
|
250
....*....|....*...
gi 1390010537 235 TDLKEEIDKMRKMIEQLK 252
Cdd:PRK03918 697 EKLKEELEEREKAKKELE 714
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
107-253 |
4.75e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.22 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 107 MSAQLAAAESRQKKL--EMEKL--QLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG4372 29 LSEQLRKALFELDKLqeELEQLreELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 183 EEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4372 105 SLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-269 |
5.29e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 74 EAGAGDKEKKPVCTNPLSilEAVMAHCKKMQERMSAqlaaaESRQKKLEMEKlqlqaLEQEHKKLAARLEEERGKnkqvv 153
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFE--EARMAHFARRQAAIKA-----EEARKADELKK-----AEEKKKADEAKKAEEKKK----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 154 lmlVKECKqlsgKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRA-KLNREEA 232
Cdd:PTZ00121 1304 ---ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEA 1376
|
170 180 190
....*....|....*....|....*....|....*..
gi 1390010537 233 httdlKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 269
Cdd:PTZ00121 1377 -----KKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
103-232 |
6.55e-08 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 52.61 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 103 MQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAARLEEERGKNKQvvlmlvkECKQLSgkviEEAQKLEDVMAKLE 182
Cdd:pfam20492 11 LEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKERLE 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1390010537 183 EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnrEEA 232
Cdd:pfam20492 69 ESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL--EEA 116
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
794-844 |
7.25e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 7.25e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 794 TPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLL 844
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-301 |
7.54e-08 |
|
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: 57.49 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 30 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKKpvctnpLSILEAVMAH 99
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK------LKNLEAELLQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 100 ckkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAAR---LEEERGKNKQVVLML-------VK 158
Cdd:pfam01576 845 ---LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEARiaqLEEELEEEQSNTELLndrlrksTL 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 159 ECKQLSGKVIEE---AQKLEDVMAKLE----EEKKKTNELEEELSAEKRRS-TEMEA---QMEKQLSEFDTEREQLRAKL 227
Cdd:pfam01576 918 QVEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKSKFKSSiAALEAkiaQLEEQLEQESRERQAANKLV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 228 NREEAHTTDLKEEIDKMRKMIEQLKRGSDsKPSLSLprKTKDRRLVSisvgTEGTVTRSVA----CQTDL--VTENADHM 301
Cdd:pfam01576 998 RRTEKKLKEVLLQVEDERRHADQYKDQAE-KGNSRM--KQLKRQLEE----AEEEASRANAarrkLQRELddATESNESM 1070
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
55-215 |
8.08e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 55 ERYGRfnlndpflalQRDYEAGAGDKEKKPvctnplsileavmahcKKMQERMSAQL----AAAESRQKKLEMEKLQLQA 130
Cdd:PRK09510 62 EQYNR----------QQQQQKSAKRAEEQR----------------KKKEQQQAEELqqkqAAEQERLKQLEKERLAAQE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 131 lEQEHKKLAARLEEErgKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME 210
Cdd:PRK09510 116 -QKKQAEEAAKQAAL--KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192
|
....*
gi 1390010537 211 KQLSE 215
Cdd:PRK09510 193 AKAAA 197
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
253-695 |
9.76e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 253 RGSDSKPSLSLPRKTKDR-RLVSISVGTEGTVTRSVACQTDLVTENAD--HMKKLPLTMPVKPSTGSPLVSANAKGSVCT 329
Cdd:PHA03247 2653 RDDPAPGRVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADppPPPPTPEPAPHALVSATPLPPGPAAARQAS 2732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 330 SATMARPGidrqasygdligasvpafPPPSANkieenGPSTGSTPDPTsSTPPLPSNAAPPTA-QTPGIAPQNSQAPPMH 408
Cdd:PHA03247 2733 PALPAAPA------------------PPAVPA-----GPATPGGPARP-ARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV 2788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 409 SLHSPCANTSLHPGLNPRIQAArfrfqgnANDPDQNGNTTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGA 488
Cdd:PHA03247 2789 ASLSESRESLPSPWDPADPPAA-------VLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPP 2848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 489 PSRPG--VPPTGDVGTHPPVGRTSLKTHGVAR--VDRGNPPPIPPKKPGLSQTPSPPHPQlkviidssrasntgakvdnK 564
Cdd:PHA03247 2849 SLPLGgsVAPGGDVRRRPPSRSPAAKPAAPARppVRRLARPAVSRSTESFALPPDQPERP-------------------P 2909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 565 TVASTPSSLPQgnrviNEENLPKSSSPQLPPKPSIDLTVAPAgcAVSALATSQVGAWPAATPGLNQPAcsdSSLVIPTTI 644
Cdd:PHA03247 2910 QPQAPPPPQPQ-----PQPPPPPQPQPPPPPPPRPQPPLAPT--TDPAGAGEPSGAVPQPWLGALVPG---RVAVPRFRV 2979
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 645 AFCSSINPVSASSCRPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 695
Cdd:PHA03247 2980 PQPAPSREAPASSTPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
90-250 |
1.07e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAARLEEERGKNKQVVLMLVKECK 161
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 162 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEkrrstemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 241
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA-------LAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*....
gi 1390010537 242 DKMRKMIEQ 250
Cdd:COG4913 443 LALRDALAE 451
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
8-253 |
1.37e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDvdTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiqERYGRFNLNDPFLALQRDYEAGAGDKEKK---- 83
Cdd:pfam17380 288 QQQEKFE--KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM---DRQAAIYAEQERMAMERERELERIRQEERkrel 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 84 --------PVCTNPLSILEAVMAHCKKMQERMSAQLAAA-------ESRQKKL-----EMEKL----------QLQALEQ 133
Cdd:pfam17380 363 erirqeeiAMEISRMRELERLQMERQQKNERVRQELEAArkvkileEERQRKIqqqkvEMEQIraeqeearqrEVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 134 EHKKLAARL-EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDvmAKLEEEKKKT--NELEEELSA---EKRRSTEMEA 207
Cdd:pfam17380 443 ERAREMERVrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR--KRAEEQRRKIleKELEERKQAmieEERKRKLLEK 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1390010537 208 QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI-DKMRKMIEQLKR 253
Cdd:pfam17380 521 EMEERQKAIYEEERRREAEEERRKQQEMEERRRIqEQMRKATEERSR 567
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
350-702 |
1.79e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 350 ASVPAFPPPSANKIEENGPStGSTPDPTSSTPPlPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQA 429
Cdd:PHA03247 2586 ARRPDAPPQSARPRAPVDDR-GDPRGPAPPSPL-PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 430 AR-FRFQGNANDPdqngnttQSPPSRDVSPTSRDNLVA-KQLAR---------NTVTQALSRFTSPQAGAPSRPGVPPTG 498
Cdd:PHA03247 2664 PRrARRLGRAAQA-------SSPPQRPRRRAARPTVGSlTSLADpppppptpePAPHALVSATPLPPGPAAARQASPALP 2736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 499 DVGTHPPVGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR 578
Cdd:PHA03247 2737 AAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 579 VINEENLPkssSPQLPPKPSIdLTVAPAGCAVSALATSQVGAWPAATPGLNQPACSDSSLVIPTTiafcsSINPVSASSC 658
Cdd:PHA03247 2817 ALPPAASP---AGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-----PARPPVRRLA 2887
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1390010537 659 RPGASDSllvTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 702
Cdd:PHA03247 2888 RPAVSRS---TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ 2928
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
694-833 |
2.49e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 55.45 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGH-TDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF 772
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 773 -ECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV 833
Cdd:PHA02876 355 kDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-272 |
2.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKqlsgKVIEEAQKLEDVMAK 180
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 181 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRKMiEQLKRGSDSKPS 260
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKADELKKA-EELKKAEEKKKA 1566
|
170
....*....|..
gi 1390010537 261 LSLPRKTKDRRL 272
Cdd:PTZ00121 1567 EEAKKAEEDKNM 1578
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-253 |
2.83e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARDLVIEALRARRKEVfIQERYGRFNLNDP-FLALQRDYEAGAGDKEKKpvcTNPLSILEAVMAHC 100
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREaLDELRAELTLLNEEAANL---RERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKnKQVVLMLVKEckqlsgkvieeaqKLEDVMAK 180
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRS-------------ELEELSEE 902
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 181 LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLEN 979
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
88-251 |
3.96e-07 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 52.52 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 88 NPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEeergknkqvvLMLVKECKQLSGKV 167
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLER---QLEELEAEAEKWEEKAR----------LALEKGREDLAREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQKLEDVMAKLEEEKKKTNELEEELsaekrrsTEMEAQMEKQLSEFDTEREQLRAKLNREEA-----------HTTD 236
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQLEEQVEKL-------KEALRQLESKLEELKAKKDTLKARAKAAKAqekvnealsgiDSDD 162
|
170
....*....|....*
gi 1390010537 237 LKEEIDKMRKMIEQL 251
Cdd:COG1842 163 ATSALERMEEKIEEM 177
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
136-240 |
4.25e-07 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 51.21 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 136 KKLAARLEEERGKNKQVVLMLVKECKQ-LSGKVIEEAQK-----LEDVMAKLEEEKKKTNELEEELsAEKRRSTEmEAQ- 208
Cdd:pfam15346 22 KRVEEELEKRKDEIEAEVERRVEEARKiMEKQVLEELERereaeLEEERRKEEEERKKREELERIL-EENNRKIE-EAQr 99
|
90 100 110
....*....|....*....|....*....|....
gi 1390010537 209 --MEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 240
Cdd:pfam15346 100 keAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
104-272 |
4.45e-07 |
|
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: 55.18 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAA---RLEEERgknkQVVLMLVKECKQLSGKVIEEAQKLEDV 177
Cdd:pfam01576 4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEeknALQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 M----AKLEEEKKKTNELEeelsAEKRRSTEMEAQMEKQLSefdtEREQLRAKLNREEAhTTDlkeeiDKMRKMIEQLKR 253
Cdd:pfam01576 77 LheleSRLEEEEERSQQLQ----NEKKKMQQHIQDLEEQLD----EEEAARQKLQLEKV-TTE-----AKIKKLEEDILL 142
|
170
....*....|....*....
gi 1390010537 254 GSDSKPSLSLPRKTKDRRL 272
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERI 161
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
163-257 |
4.90e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.83 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 163 LSGKVIEEAQ--------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLnREEAH- 233
Cdd:PRK00409 499 LPENIIEEAKkligedkeKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQq 577
|
90 100
....*....|....*....|....*
gi 1390010537 234 -TTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:PRK00409 578 aIKEAKKEADEIIKELRQLQKGGYA 602
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
313-712 |
5.24e-07 |
|
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: 54.54 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 313 STGSPLVSANAKGSVCTSATMARPGIdrqASYGDLIGASVPAFPPPSANKIEENGPsTGSTPDPTSSTPPLPSNAAPPTa 392
Cdd:pfam05109 414 TTTHKVIFSKAPESTTTSPTLNTTGF---AAPNTTTGLPSSTHVPTNLTAPASTGP-TVSTADVTSPTPAGTTSGASPV- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 393 qTPGIAPQN----SQAP----PMHSLHSPCAN-TSLHPGLNPRIQAARFRFQGNANdpDQNGNTTQSPPSRDVSP---TS 460
Cdd:pfam05109 489 -TPSPSPRDngteSKAPdmtsPTSAVTTPTPNaTSPTPAVTTPTPNATSPTLGKTS--PTSAVTTPTPNATSPTPavtTP 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 461 RDNLVAKQLARNTVTQALSRFTsPQAGAPSRPGVPPTGDVGTH-------------PPVGRTSLKTHGVARVDRGNPPPI 527
Cdd:pfam05109 566 TPNATIPTLGKTSPTSAVTTPT-PNATSPTVGETSPQANTTNHtlggtsstpvvtsPPKNATSAVTTGQHNITSSSTSSM 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 528 PPKKPGLSQTPSP---------------PHPQ-LKVIIDSSRASNTGAKVDNKTVASTPSSLPQ----GNRVIN----EE 583
Cdd:pfam05109 645 SLRPSSISETLSPstsdnstshmplltsAHPTgGENITQVTPASTSTHHVSTSSPAPRPGTTSQasgpGNSSTStkpgEV 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 584 NLPKSSSPQLPPKPSidltvAPAGCAVSA-LATSQVGAWPAATPGLNQPACSDSSLVIPTTIAFCSSINP---VSASSCR 659
Cdd:pfam05109 725 NVTKGTPPKNATSPQ-----APSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPrtrYNATTYL 799
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 660 PGASDSLLvtASGWSPSLTPLLMSGG--PAPLAGRP------TLLQQAAAQGNVTLLSMLL 712
Cdd:pfam05109 800 PPSTSSKL--RPRWTFTSPPVTTAQAtvPVPPTSQPrfsnlsMLVLQWASLAVLTLLLLLV 858
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
93-413 |
5.55e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGK-NKQVVLMlvkeckQLSG------ 165
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERARAL------YRSGgsvsyl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 166 -------------------KVIEEAQKleDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 226
Cdd:COG3883 106 dvllgsesfsdfldrlsalSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 227 LNREEAhttDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTEnadhmkklpl 306
Cdd:COG3883 184 LAQLSA---EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 307 tmpvkpstGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSN 386
Cdd:COG3883 251 --------AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAV 322
|
330 340
....*....|....*....|....*..
gi 1390010537 387 AAPPTAQTPGIAPQNSQAPPMHSLHSP 413
Cdd:COG3883 323 VGGASAGGGGGSGGGGGSSGGGSGGGG 349
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-237 |
5.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKvIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDE----LKGEIGRLEKE-LEQAEEELDELQDRLEAAEDL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1390010537 189 NELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDL 237
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-253 |
7.81e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAA--ESRQKKLEMEKLQLQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLE 175
Cdd:COG1196 219 KEELKELEAELLLLklRELEAELEELEAELEELEAELEELEAELaelEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 176 DVMAKLEEEKKKTNELE---EELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:COG1196 299 RLEQDIARLEERRRELEerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
.
gi 1390010537 253 R 253
Cdd:COG1196 379 E 379
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
117-251 |
7.98e-07 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 50.42 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 117 RQKKLEMEKLQLQALEQEhkklaarlEEERgknkqvvlmLVKEckQLSGKVIEEAQKLEDVMAKLEEEKKKTnelEEELS 196
Cdd:pfam05672 21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRRE---EEERQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 197 AEKRRSTEMEAQMEKQlsefdterEQLRAKLNREEAHTTdLKEEIDKMRKMIEQL 251
Cdd:pfam05672 79 RKAEEEAEEREQREQE--------EQERLQKQKEEAEAK-AREEAERQRQEREKI 124
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
711-763 |
8.02e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 8.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 711 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPL 763
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
728-832 |
8.17e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 52.68 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 728 SALYSAAKNGHTDCVRLLL----SAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQ-TPLYLACKN 802
Cdd:PHA02884 35 NILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|
gi 1390010537 803 GNKECIKLLLEAGTNRSVKTTDGWTPVHAA 832
Cdd:PHA02884 115 GCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
734-812 |
8.25e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 8.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 734 AKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLL 812
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-258 |
8.35e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAARLEEERG-----KNKQVVLMLV------------KECKQLSGK 166
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 167 VIEEAQKLEDvmaKLEEEKKKTNELEEeLSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKM-- 244
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdf 552
|
170
....*....|....*..
gi 1390010537 245 ---RKMIEQLKRGSDSK 258
Cdd:TIGR04523 553 elkKENLEKEIDEKNKE 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-271 |
9.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSA-QLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDvm 178
Cdd:PTZ00121 1528 KKAEEAKKAdEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEED--------------KNMALRKAEEAKKAEE-- 1591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 179 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER---EQLRAKLNREEAHTTDLK--EEIDKMRKMIEQLKR 253
Cdd:PTZ00121 1592 -ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKkkvEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKA 1670
|
170
....*....|....*...
gi 1390010537 254 GSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK 1688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
93-251 |
9.14e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKECKQLSGKvIEEAQ 172
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEE-IEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 ----KLEDVMAKLEEEKKKT----NELE---EELSAEKRRSTEMEAQMEK--QLSEFdteREQLRAKLNREEAHTTDLKE 239
Cdd:PRK03918 245 keleSLEGSKRKLEEKIRELeeriEELKkeiEELEEKVKELKELKEKAEEyiKLSEF---YEEYLDELREIEKRLSRLEE 321
|
170
....*....|..
gi 1390010537 240 EIDKMRKMIEQL 251
Cdd:PRK03918 322 EINGIEERIKEL 333
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-271 |
1.08e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQE-RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA 179
Cdd:TIGR02169 218 KEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR--GSDS 257
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVD 377
|
170
....*....|....
gi 1390010537 258 KPSLSLPRKTKDRR 271
Cdd:TIGR02169 378 KEFAETRDELKDYR 391
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
127-252 |
1.09e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 127 QLQALEQEHKKLAARLEEErgknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 206
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQ-----QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQR 580
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 207 AQMEKQLSEFDTEREQLRAK----------LNREEAHT----TDLKEEIDKMRKMIEQLK 252
Cdd:COG3096 581 SELRQQLEQLRARIKELAARapawlaaqdaLERLREQSgealADSQEVTAAMQQLLERER 640
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
113-258 |
1.15e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 113 AAESRQKKLEMEKLQ--LQALE--QEHKKLaaRLEEERgknkqvvlMLVKECKQLSgKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG1340 101 LAELNKAGGSIDKLRkeIERLEwrQQTEVL--SPEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 189 NELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKlnREEAHTT-----------------------DLKEEID 242
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247
|
170
....*....|....*.
gi 1390010537 243 KMRKMIEQLKRGSDSK 258
Cdd:COG1340 248 KLRKKQRALKREKEKE 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
127-226 |
1.39e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 127 QLQALEQEHKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKkktneleEELSAEKRRSTEME 206
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAER-----LLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERR 581
|
90 100
....*....|....*....|
gi 1390010537 207 AQMEKQLSEFDTEREQLRAK 226
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAAR 601
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
694-830 |
1.52e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.09 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQ-VNAADKN----GFTPLCAAAA 768
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 769 QGHFECVELLISYDANINHA-ADG-------------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVH 830
Cdd:cd22192 99 NQNLNLVRELIARGADVVSPrATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-232 |
1.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL--------------EELEEALAELEEEEEEEEEALEE 446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1390010537 184 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
21-201 |
2.00e-06 |
|
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: 52.07 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 21 SELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRdyeagAGDKEKKPVCTNP---------LS 91
Cdd:COG4942 65 AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR-----LGRQPPLALLLSPedfldavrrLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 92 ILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKV---I 168
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaelQ 219
|
170 180 190
....*....|....*....|....*....|...
gi 1390010537 169 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
105-252 |
2.13e-06 |
|
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: 52.87 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAARLEEERG--KNKQVVLMLVKECK---------------QLSGKV 167
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeqleqesrerQAANKL 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQK-LEDVMAKLEEEKKKTNELEEElsAEKrrSTEMEAQMEKQLSEfdTEREQLRA-----KLNREeahTTDLKEEI 241
Cdd:pfam01576 997 VRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKLQRE---LDDATESN 1067
|
170
....*....|.
gi 1390010537 242 DKMRKMIEQLK 252
Cdd:pfam01576 1068 ESMNREVSTLK 1078
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
107-252 |
2.46e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 107 MSAQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLEEERGKnkqvvlmlVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG1340 6 LSSSLEELEEKIEELREEieelKEKRDELNEELKELAEKRDELNAQ--------VKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 183 EEK----KKTNELEEEL------SAEKRRSTEMEAQMEKQLSEFdtEREQLRAKLNREE-----AHTTDLKEEIDKMRKM 247
Cdd:COG1340 78 EERdelnEKLNELREELdelrkeLAELNKAGGSIDKLRKEIERL--EWRQQTEVLSPEEekelvEKIKELEKELEKAKKA 155
|
....*
gi 1390010537 248 IEQLK 252
Cdd:COG1340 156 LEKNE 160
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
168-253 |
2.78e-06 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 47.95 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT-----EREQLRA--KLNREEAHTTDLKEE 240
Cdd:pfam13863 2 LEKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKflkenDAKRRRAlkKAEEETKLKKEKEKE 81
|
90
....*....|...
gi 1390010537 241 IDKMRKMIEQLKR 253
Cdd:pfam13863 82 IKKLTAQIEELKS 94
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
782-832 |
3.02e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 3.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 782 DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAA 832
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
115-252 |
3.05e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 115 ESRQKKLEmEKLQLQALEQEHKKLAA--RLEEERGKNKQVVLM-------LVKECKQLSGKVIEEAQKLEDVMAKLEEEK 185
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEviKEIKRRIERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 186 KKTNELEEELsaEKRRstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:PRK03918 224 EKLEKEVKEL--EELK--EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8-248 |
3.10e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDVDTLSKsELRMLLSVMEGELEARDlviEALRARRKEV-FIQERYGRFnlndpflaLQRDYEAGAGDKEKKPVC 86
Cdd:pfam12128 285 SAELNQLLRTLDD-QWKEKRDELNGELSAAD---AAVAKDRSELeALEDQHGAF--------LDADIETAAADQEQLPSW 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 87 TNPLSILEAVMA----------------------HCKKMQERMSAQLAAA-ESRQKKLEMEKLQLQALEQE-HKKLAARL 142
Cdd:pfam12128 353 QSELENLEERLKaltgkhqdvtakynrrrskikeQNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQALESElREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 143 EEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEdvmakLEEEKKKTNELEEELsaEKRRSTEMEAQMEkqLSEFDTEREQ 222
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ--EAANAEVERLQSE--LRQARKRRDQ 503
|
250 260
....*....|....*....|....*.
gi 1390010537 223 LRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam12128 504 ASEALRQASRRLEERQSALDELELQL 529
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
739-845 |
3.24e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 51.76 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 739 TDCVRLLLSAEAQVNAADKNGFTPLCAAAA-----QGHFECVELLISYDANINHAADGGQTPLYLACKNG---NKECIKL 810
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 1390010537 811 LLEAGTNRSVKTTDGWTPVHAAVDTGN---VDSLKLLM 845
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
696-781 |
3.42e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 696 LQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECV 775
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
....*.
gi 1390010537 776 ELLISY 781
Cdd:PTZ00322 165 QLLSRH 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-258 |
4.09e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKLQLQALEQEHKKLAARLEeergkNKQvvlmlvKECKQLSGKVIEEAQKLEDVMAKLEEEKKK-----TNELE 192
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLS-----EKQ------KELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELK 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 193 EELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
105-256 |
4.15e-06 |
|
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: 51.71 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAaesrqKKLEMEKLqLQALEqehkklaARLEEERGKNKQvvlmLVKECKQLSGKVI--------EEA--QKL 174
Cdd:pfam01576 60 EEMRARLAA-----RKQELEEI-LHELE-------SRLEEEEERSQQ----LQNEKKKMQQHIQdleeqldeEEAarQKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 --EDV-----MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL-----KEEid 242
Cdd:pfam01576 123 qlEKVtteakIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLeerlkKEE-- 200
|
170
....*....|....
gi 1390010537 243 KMRKMIEQLKRGSD 256
Cdd:pfam01576 201 KGRQELEKAKRKLE 214
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-253 |
4.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkecKQLSGKVIEEAQKLEDVMAKLEEEKKKT 188
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---------EELAERLAEEELELEEALLAEEEEEREL 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 189 NELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| APG6_N |
pfam17675 |
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ... |
100-233 |
5.28e-06 |
|
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.
Pssm-ID: 465452 [Multi-domain] Cd Length: 127 Bit Score: 47.21 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 100 CKKMQERMSAQLAAAES-RQ------KKLEMEKL-QLQALEQEHKKLaaRLEEERgknkqvvlmLVKECKQLSgkviEEA 171
Cdd:pfam17675 7 TDLLLEELDKQLEDAEKeRDayisflKKLEKETPeELEELEKELEKL--EKEEEE---------LLQELEELE----KER 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELSAEKRrstemeaQMEKQLSEFDTEREQLRAKLNREEAH 233
Cdd:pfam17675 72 EELDAELEALEEELEALDEEEEEFWREYN-------ALQLQLLEFQDERDSLEAQYEHALNQ 126
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
101-253 |
5.70e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 50.42 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSaQLAAAESRQKKLEMEKLQLQALEQEHKKL--AARL-EEERGKNK---QVVLMLVKEckqlsgkvIEEAQKL 174
Cdd:pfam15558 87 KQVIEKES-RWREQAEDQENQRQEKLERARQEAEQRKQcqEQRLkEKEEELQAlreQNSLQLQER--------LEEACHK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 EDVMAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRAKLNRE---EAHTTDLKEEIDKMRKMIEQ 250
Cdd:pfam15558 158 RQLKEREEQKKVQENNLSELLNHQARkVLVDCQAKAEELLRRLSLEQSLQRSQENYEqlvEERHRELREKAQKEEEQFQR 237
|
...
gi 1390010537 251 LKR 253
Cdd:pfam15558 238 AKW 240
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
108-253 |
5.78e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 108 SAQLAAAESRQKK-LEMEKLQLQALEQEhKKLAARLEEERGKNKqvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKK 186
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKE-ALLEAKEEIHKLRNE-----FEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 187 KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR------EEAhttdlKEEIdkMRKMIEQLKR 253
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEA-----KEIL--LEKVEEEARH 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
114-253 |
6.05e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 114 AESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIE--------------EAQKLEDVMA 179
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEiekeieqleqeeekLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 180 KLEeekkktnELEEELSAEKRRSTEMEA---QMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKMIEQL 251
Cdd:TIGR02169 745 DLS-------SLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREI 817
|
..
gi 1390010537 252 KR 253
Cdd:TIGR02169 818 EQ 819
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
101-236 |
6.22e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEME------KLQLQALEQEHKKLAARLEE---ERGKNKQVVLMLVKECKQLSGKVIEEA 171
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRaelkelRKEAEEIHKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQ 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELSaeKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTD 236
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELK--KLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTE 285
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
133-252 |
8.25e-06 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 49.59 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 133 QEHKKLAARLEEERGKNKQVVLMLVKECKqlSGKVIEEA-----QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 207
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQ--SKEAVEEAilqtdQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQ 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1390010537 208 QMEKQLSEFDTEREQLRAKLNREEAHttdLKEEIDKM--RKMIEQLK 252
Cdd:pfam02841 233 MMEAQERSYQEHVKQLIEKMEAEREQ---LLAEQERMleHKLQEQEE 276
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
90-252 |
8.69e-06 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 48.25 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 90 LSILEAVMAHCKKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKLAAR-LEEERGKNKQVVLMLVKECKQL 163
Cdd:pfam14662 7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQKEKlLEEELEDLKLIVNSLEEARRSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 164 SGK---VIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEE 240
Cdd:pfam14662 87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166
|
170
....*....|..
gi 1390010537 241 IDKMRKMIEQLK 252
Cdd:pfam14662 167 VEEYSSIEEELR 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
128-253 |
9.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 128 LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEA 207
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1390010537 208 QmeKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4717 124 L--LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE 167
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
101-258 |
1.09e-05 |
|
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: 50.49 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESR----QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKE-------CKQLSGKVIE 169
Cdd:pfam05483 91 KKWKVSIEAELKQKENKlqenRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD----LIKEnnatrhlCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 170 EAQKledvMAKLEEEKKKTNELEEELSaekrrstemeAQMEKQLSEFDTEREQlrAKLNREEAHTTdLKEEIDKMRKMIE 249
Cdd:pfam05483 167 SAEK----TKKYEYEREETRQVYMDLN----------NNIEKMILAFEELRVQ--AENARLEMHFK-LKEDHEKIQHLEE 229
|
....*....
gi 1390010537 250 QLKRGSDSK 258
Cdd:pfam05483 230 EYKKEINDK 238
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
695-844 |
1.11e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 695 LLQQAAAQGNVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFEC 774
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 775 VELLISYDANINHaadgGQTPLYLACKNGNKECIKLLLEAGTnrSVKTTDGW--TPVHAAVDTGNVDSL--KLL 844
Cdd:PHA02876 227 IKAIIDNRSNINK----NDLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLvpKLL 294
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
115-245 |
1.12e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 47.38 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 115 ESRQKKLEMEKLQLQAlEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQ-KLEDVMAKLEEEKKKTNELEE 193
Cdd:pfam11600 5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 194 ELSAEKRRSTEmEAQMEKQlsefdterEQLRAKL--NREEAHTTDLKEEIDKMR 245
Cdd:pfam11600 80 KEKAEKLRLKE-EKRKEKQ--------EALEAKLeeKRKKEEEKRLKEEEKRIK 124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-253 |
1.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEmEKLQLQALEQEHKKL--------------AARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:COG4717 347 EELQELLREAEELE-EELQLEELEQEIAALlaeagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 --EDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK-----QLSEFDTEREQLRAKLNR--EEAHTTDLKEEIdkMR 245
Cdd:COG4717 426 deEELEEELEELEEELEELEEELEELREELAELEAELEQleedgELAELLQELEELKAELRElaEEWAALKLALEL--LE 503
|
....*...
gi 1390010537 246 KMIEQLKR 253
Cdd:COG4717 504 EAREEYRE 511
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
711-787 |
1.18e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.66 E-value: 1.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 711 LLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINH 787
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
99-271 |
1.23e-05 |
|
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: 50.11 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 99 HCKKMQERMSAQLAAAESRQKKL--EMEKLQlQALEQEHKKLAARL---EEERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVR-EEFIQKGDEVKCKLdksEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
170
....*....|....*...
gi 1390010537 254 GSDSKPSLslpRKTKDRR 271
Cdd:pfam05483 683 IADEAVKL---QKEIDKR 697
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
696-833 |
1.25e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 50.08 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 696 LQQAAAQGNVTLLSMLLNEEGLDInyscEDGHSALYSAAKNGH---TDCVRLLLSAEAQ------VNAADKNGF----TP 762
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYVdavEAILLHLLAAFRKsgplelANDQYTSEFtpgiTA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 763 LCAAAAQGHFECVELLISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAGTNrsVKTTD--GW 826
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslGN 209
|
....*..
gi 1390010537 827 TPVHAAV 833
Cdd:TIGR00870 210 TLLHLLV 216
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
100-257 |
1.51e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 100 CKKMQERMSAQLAAAES--------RQKKLEMEKLQLQALEQEHKKLAARLEEERGKN--KQVVLMLVKE---CKQLSGK 166
Cdd:pfam05622 213 YKKLEEKLEALQKEKERliierdtlRETNEELRCAQLQQAELSQADALLSPSSDPGDNlaAEIMPAEIREkliRLQHENK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 167 VIEEAQ------KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQME---KQLSEFDTERE---QLRAKLNREEAHT 234
Cdd:pfam05622 293 MLRLGQegsyreRLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEelqKALQEQGSKAEdssLLKQKLEEHLEKL 372
|
170 180
....*....|....*....|...
gi 1390010537 235 TDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:pfam05622 373 HEAQSELQKKKEQIEELEPKQDS 395
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
141-253 |
1.75e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 141 RLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----------LEEELSAEKRRSTEMEAQM 209
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREeleqareeleqLEEELEQARSELEQLEEEL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1390010537 210 E---KQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4372 83 EelnEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
101-251 |
1.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 177
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEaeaEEKREAAAEAEEEAEEAREEV----AELNSKLAELKERIESLERI 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 178 MAKLEEEKKKTNELEEElsAEKRRS-TEMEAQMEKQLSEFDTEREQLRAKLnrEEAHTTDLKEEIDKMRKMIEQL 251
Cdd:PRK02224 595 RTLLAAIADAEDEIERL--REKREAlAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQV 665
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-283 |
2.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVLMLVKEckqlsgkvIEEAQKLEDVMA 179
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEALRAAAELAAQLEELEEAEEAL--------LERLERLEEELE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR---KMIEQLKRGSD 256
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLLLLEAEADYE 504
|
170 180
....*....|....*....|....*...
gi 1390010537 257 SKPSLSLPRKTKD-RRLVSISVGTEGTV 283
Cdd:COG1196 505 GFLEGVKAALLLAgLRGLAGAVAVLIGV 532
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
792-817 |
2.08e-05 |
|
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: 42.57 E-value: 2.08e-05
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
168-258 |
2.31e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 47.72 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQ-KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHTTdlKEEIDKMRK 246
Cdd:pfam00261 10 LDEAEeRLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKL------EEAEKA--ADESERGRK 81
|
90
....*....|..
gi 1390010537 247 MIEQLKRGSDSK 258
Cdd:pfam00261 82 VLENRALKDEEK 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
93-246 |
2.32e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEErgknKQVVLMLVKECKQlsgKVIEEAQ 172
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALEN---KIEDDEE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLEDVMAKLEEEKKK---TNEL-EEELSAEKRRSTEMEAQMEkqlsEFDTEREQLR---AKLNREEahTTDLKEEIDKMR 245
Cdd:TIGR02168 969 EARRRLKRLENKIKElgpVNLAaIEEYEELKERYDFLTAQKE----DLTEAKETLEeaiEEIDREA--RERFKDTFDQVN 1042
|
.
gi 1390010537 246 K 246
Cdd:TIGR02168 1043 E 1043
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
758-786 |
2.39e-05 |
|
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: 42.57 E-value: 2.39e-05
10 20
....*....|....*....|....*....
gi 1390010537 758 NGFTPLCAAAAQGHFECVELLISYDANIN 786
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
758-786 |
2.42e-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. 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: 42.66 E-value: 2.42e-05
10 20 30
....*....|....*....|....*....|
gi 1390010537 758 NGFTPL-CAAAAQGHFECVELLISYDANIN 786
Cdd:pfam00023 1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVN 30
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-246 |
2.52e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEME----KLQLQALEQEHKKLAARLE-----EERGKNKQVVLMLVKECKQLSgKVIEEAQKLEDVMA 179
Cdd:COG4913 610 AKLAALEAELAELEEElaeaEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELE-AELERLDASSDDLA 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 180 KLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR-EEAHTTDLKEEIDKMRK 246
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFA 756
|
|
| PHA03369 |
PHA03369 |
capsid maturational protease; Provisional |
200-633 |
2.79e-05 |
|
capsid maturational protease; Provisional
Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 48.84 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 200 RRSTEMEAQMEKQLSEFDTEREQlraKLNREEAHTTDLKEEIDKMRKMIEQLKrgsDSKPSLSLPRKTKDRRLVS--ISV 277
Cdd:PHA03369 257 RQGEAPLNALLEILKAKNAEMPG---TLNPSFGSSDESPEWKTFYEALADQLN---NLYKLLRTIYKHKDETVIEqyLIE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 278 GTEGTVTrsvacqtdlVTENADHMKKLPLTMPVKPStgSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPP 357
Cdd:PHA03369 331 GRKLFST---------INGLKAHNEILKTASLTAPS--RVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 358 PSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAP-PMHSLhspcantsLHPGLNPRIQAARFRFQG 436
Cdd:PHA03369 400 MTAYPPVPQFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPiSMANM--------VYPGHPQEHGHERKRKRG 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 437 NANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSrPGVPPTGDVGTHPPVGRTSLKT--H 514
Cdd:PHA03369 472 GELKEELIETLKLVKKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAA-ANIEPNCSADAAAPATKRARPEtkT 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 515 GVARVDRgnPPPIPPKKPGLSQTPSPPHPQLKVIIdsSRASNTGAKVDN--KTVASTPSSLPQGNRVINEENLPKSSSPQ 592
Cdd:PHA03369 551 ELEAVVR--FPYQIRNMESPAFVHSFTSTTLAAAA--GQGSDTAEALAGaiETLLTQASAQPAGLSLPAPAVPVNASTPA 626
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1390010537 593 LPPKPSIDLTVAPAGCAVSALATSQvgawPAATPGLNQPAC 633
Cdd:PHA03369 627 STPPPLAPQEPPQPGTSAPSLETSL----PQQKPVLSKGAF 663
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
96-252 |
2.84e-05 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 48.90 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 96 VMAHCKKMQERMSA-QLAAAESRQKKLEMEKLQLQaleqehkKLAArleEERGKNKQVVLmlvKECKQLSGKVIEEA-QK 173
Cdd:pfam05911 5 VKQHAKVAEEAVSGwEKAEAEALALKQQLESVTLQ-------KLTA---EERAAHLDGAL---KECMQQLRNVKEEQeQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 LEDV-MAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNRE----EAHTTDLKEEIDKMRKMI 248
Cdd:pfam05911 72 IHDVvLKKTKEWEKIKAELEAKLVETEQELLRAAAE-NDALSRSLQERENLLMKLSEEksqaEAEIEALKSRLESCEKEI 150
|
....
gi 1390010537 249 EQLK 252
Cdd:pfam05911 151 NSLK 154
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-207 |
3.42e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDVDTLSKSELRmlLSVMEGELEARDLVIEALRARRKEVFIQERYgrfnLNDPFLALQRDYEAGAGDKEKKPV-- 85
Cdd:TIGR02169 797 QAELSKLEEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIENLNGKKEELEEel 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 86 --CTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKQV----------- 152
Cdd:TIGR02169 871 eeLEAALRDLESRLGDLKKERDELEAQLRELERKIEELE---AQIEKKRKRLSELKAKLEALEEELSEIedpkgedeeip 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 153 ----VLMLVKECKQlsgKVIEEAQKLEDV---------------------MAKLEEEKKKTNELEEELSaEKRRSTEMEA 207
Cdd:TIGR02169 948 eeelSLEDVQAELQ---RVEEEIRALEPVnmlaiqeyeevlkrldelkekRAKLEEERKAILERIEEYE-KKKREVFMEA 1023
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
80-302 |
3.50e-05 |
|
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: 48.89 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 80 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVK- 158
Cdd:TIGR00606 216 KEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKv 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 159 ------ECKQL----SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTERE--QL 223
Cdd:TIGR00606 296 fqgtdeQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqeHIRARDSLIQslAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 224 RAKLNREEaHTTDLKEEID-----KMRKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGtVTRSVACQTDLVTENA 298
Cdd:TIGR00606 376 RLELDGFE-RGPFSERQIKnfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKG-LGRTIELKKEILEKKQ 453
|
....
gi 1390010537 299 DHMK 302
Cdd:TIGR00606 454 EELK 457
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
704-852 |
3.55e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.48 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 704 NVTLLSMLLnEEGLDINYSCEDGHSALYSAAKNGHTD--CVRLLLSAEAQVNAADKNGFTPLCAAAAqgHFECVELLISY 781
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLP 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 782 ----DANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHRIPAH 852
Cdd:PHA03095 243 lliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
115-253 |
3.95e-05 |
|
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: 48.81 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 115 ESRQKKLEMEKLQLQALEQEHKK--LAAR---LEEERGKNKQVVLMLVKECKQLSGKVIE-EAQKLEDVMAKLEEEKKKT 188
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEylLYLDylkLNEERIDLLQELLRDEQEEIESSKQEIEkEEEKLAQVLKENKEEEKEK 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 189 NELEEELS--AEKRRSTEMEAQMEKQLSEFDTEREQL-RAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam02463 282 KLQEEELKllAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
46-252 |
3.97e-05 |
|
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: 48.43 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 46 ARRKEVFIQERygrfNLNDPFLALQRDYEAgagDKEKKPVCTNPLSILEAVMAHCKKMQERMSA---QLAAAESrQKKLE 122
Cdd:TIGR00618 365 TSIREISCQQH----TLTQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKK-QQELQ 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 123 MEKLQLQAL------------EQEHKKLAARLEEERGK--NKQVVLMLVKECKQLSGKVIEEAQ---------------- 172
Cdd:TIGR00618 437 QRYAELCAAaitctaqcekleKIHLQESAQSLKEREQQlqTKEQIHLQETRKKAVVLARLLELQeepcplcgscihpnpa 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 ---------------KLEDVMAKLEEEKKKTnelEEELSAEKRRSTEMEAQMEkqlsEFDTEREQLRAKLNReeahttdL 237
Cdd:TIGR00618 517 rqdidnpgpltrrmqRGEQTYAQLETSEEDV---YHQLTSERKQRASLKEQMQ----EIQQSFSILTQCDNR-------S 582
|
250
....*....|....*
gi 1390010537 238 KEEIDKMRKMIEQLK 252
Cdd:TIGR00618 583 KEDIPNLQNITVRLQ 597
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
69-253 |
4.88e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.76 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 69 LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL-QLQALEQEHKKLAARLEEERG 147
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLtELQQLLEDANRRKNELETQNR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 148 KNKQVVLMLVKECKQLSGKVIEEAQKLEDVMA---KLEEEKKKTNELEEELSAEKRRSTEMEAqmeKQLSEFDTEREQLR 224
Cdd:pfam05622 329 LANQRILELQQQVEELQKALQEQGSKAEDSSLlkqKLEEHLEKLHEAQSELQKKKEQIEELEP---KQDSNLAQKIDELQ 405
|
170 180
....*....|....*....|....*....
gi 1390010537 225 AKLNREEahttdlkeeiDKMRKMIEQLKR 253
Cdd:pfam05622 406 EALRKKD----------EDMKAMEERYKK 424
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
769-848 |
5.02e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.14 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 769 QGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLKLLMYHR 848
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
172-272 |
5.13e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELS--AEKRRS-----TEMEAQMEKQLSEFDTEREQLR-AKLNREEahttdLKEEIDK 243
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKelAEKRDElnaqvKELREEAQELREKRDELNEKVKeLKEERDE-----LNEKLNE 89
|
90 100
....*....|....*....|....*....
gi 1390010537 244 MRKMIEQLKRGSDSKPSLSLPRKTKDRRL 272
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKEI 118
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
110-257 |
5.18e-05 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.21 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 110 QLAAAESRQKKLEMEklqlqaLEQEhKKLAARLEEergknkQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTN 189
Cdd:pfam04012 44 ALAQTIARQKQLERR------LEQQ-TEQAKKLEE------KAQAALTKGNEELAREALAEKKSLEKQAEALETQLAQQR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 190 EleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNreeahTTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:pfam04012 111 S--------------AVEQLRKQLAALETKIQQLKAKKN-----LLKARLKAAKAQEAVQTSLGSLST 159
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
97-251 |
5.31e-05 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 45.09 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMqerMSAQLAAA-ESRQKKLEMEklqLQALEQEHKKLAARLEEERGknkqvvlmLVKECKQLSGKVIEEAqkle 175
Cdd:TIGR01144 9 VWFCMKY---VWPPLAKAiETRQKKIADG---LASAERAKKEAALAQKKAQV--------ILKEAKDEAQEIIENA---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 176 dvmakleeeKKKTNELEEELSAEKRrsTEMEAQMEKQLSEFDTEREQLRAKLNREeahTTDL---------KEEIDKM-- 244
Cdd:TIGR01144 71 ---------NKRGSEILEEAKAEAR--EEREKIKAQARAEIEAEKEQAREELRKQ---VADLsvlgaekiiERNIDKQaq 136
|
....*..
gi 1390010537 245 RKMIEQL 251
Cdd:TIGR01144 137 KDLIDKL 143
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
22-251 |
5.55e-05 |
|
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: 48.25 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSI-LEAVMAHC 100
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIR----ELEAQISELQEDLESERAARNKAEKQRRDLGEeLEALKTEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQlaaAESRQKKlEMEKLQLQ-ALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkviEEAQKLEDVMA 179
Cdd:pfam01576 309 EDTLDTTAAQ---QELRSKR-EQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK----RNKANLEKAKQ 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 180 KLEEEkkkTNELEEELSAEKRRSTEMEAQMEKQlsefDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:pfam01576 381 ALESE---NAELQAELRTLQQAKQDSEHKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESV 445
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
104-246 |
5.62e-05 |
|
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: 48.04 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQ-------EHKKLAARLEEErgknkQVVLMLVKEC-KQLSGKVIEEAQKLE 175
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQlalmefaKKKSLHGKAELL-----TLRSQLLTLCtPCMPDTYHERKQVLE 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 176 DVMAKLEEEKKKTNELEEELSaEKRRSTEMEAQMEKQLSEFDTEREQLRAklnrEEAHTTDLKEEIDKMRK 246
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLT-QKREAQEEQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARK 291
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
750-799 |
5.97e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 5.97e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1390010537 750 AQVNAADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA 799
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
101-271 |
6.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKlEMEKLQLQAlEQEHKKLAARLEEERGKNKQVVLMLVKECKqlsgKVIEEAQKLEDVM-- 178
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAK-KADEAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAK----KKADEAKKAEEAKka 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 179 --AKLEEEKKKTNEL---EEELSAEK-RRSTEMEAQMEKQLSEFDTEREQLRAKLNR--------EEAHTTDLKEEIDKM 244
Cdd:PTZ00121 1525 deAKKAEEAKKADEAkkaEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRkaeeakkaEEARIEEVMKLYEEE 1604
|
170 180
....*....|....*....|....*...
gi 1390010537 245 RKM-IEQLKRGSDSKPSLSLPRKTKDRR 271
Cdd:PTZ00121 1605 KKMkAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-251 |
6.53e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 112 AAAESRQKKLEMEkLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKTNEL 191
Cdd:PRK02224 469 TIEEDRERVEELE-AELEDLEEEVEEVEERLER-----------------------AEDLVEAEDRIERLEERREDLEEL 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 192 EEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN---------REEAHT-----TDLKEEIDKMRKMIEQL 251
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAeaeeeaeeaREEVAElnsklAELKERIESLERIRTLL 598
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
111-258 |
6.84e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.90 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 111 LAAAESRQKKLEMEKLQLQALE---QEHKKLAARLEEERGKNKQVVLM----LVKECKQLSGKVIEEAQKLEDV------ 177
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEervEALNELGEQLIEEGHPDAEEIQErleeLNQRWEELRELAEERRQRLEEAldlqqf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAKLEEEKKKTNELEEELSAEKRRS--TEMEAQMEKqLSEFDTEREQLRAKLNR------------EEAHTTDLKEEIDK 243
Cdd:cd00176 112 FRDADDLEQWLEEKEAALASEDLGKdlESVEELLKK-HKELEEELEAHEPRLKSlnelaeelleegHPDADEEIEEKLEE 190
|
170
....*....|....*
gi 1390010537 244 MRKMIEQLKRGSDSK 258
Cdd:cd00176 191 LNERWEELLELAEER 205
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
296-433 |
7.30e-05 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 47.26 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 296 ENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIgasVPAFPPPSANKIE--ENGPSTGST 373
Cdd:PHA03291 151 EGATNASLFPLGLAAFPAEGTLAAPPLGEGSADGSCDPALPLSAPRLGPADVF---VPATPRPTPRTTAspETTPTPSTT 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 374 PDPTSSTPPLPS-NAAPPTAQTPGIAPQNSQAPPMHSLHSPCANTSlhpglnPRIQAARFR 433
Cdd:PHA03291 228 TSPPSTTIPAPStTIAAPQAGTTPEAEGTPAPPTPGGGEAPPANAT------PAPEASRYE 282
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-251 |
7.66e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 184 EKKKTNELEEE-------LSAEKRRSTEMEAQMEK-------QLSEFDTEREQLRAkLNREEAhttDLKEEIDKMRKMIE 249
Cdd:COG1196 744 EEELLEEEALEelpeppdLEELERELERLEREIEAlgpvnllAIEEYEELEERYDF-LSEQRE---DLEEARETLEEAIE 819
|
..
gi 1390010537 250 QL 251
Cdd:COG1196 820 EI 821
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
149-250 |
8.09e-05 |
|
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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 44.11 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 149 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEE---LSAEKRRstEMEAQMEKQLSEFDTEREQLR 224
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKElQKLKEKLQKDaatLSEAARE--KKEKELQKKVQEFQRKQQKLQ 82
|
90 100
....*....|....*....|....*.
gi 1390010537 225 AKLNREEAhttdlkEEIDKMRKMIEQ 250
Cdd:smart00935 83 QDLQKRQQ------EELQKILDKINK 102
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
104-207 |
8.66e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGkvIEEAQKLEDVMAKLEE 183
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME--MAEEERLEYQRQKQEA 486
|
90 100
....*....|....*....|....
gi 1390010537 184 EKKKtneleeELSAEKRRSTEMEA 207
Cdd:pfam15709 487 EEKA------RLEAEERRQKEEEA 504
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
22-252 |
8.67e-05 |
|
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: 47.20 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGAGDKEKKPVCTNPLSilEAV 96
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDR--EQW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam07888 72 ERQRRELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 LEDV---------MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:pfam07888 152 LERMkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNsLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
....*....
gi 1390010537 244 MRKMIEQLK 252
Cdd:pfam07888 232 NEALLEELR 240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
103-253 |
8.74e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 103 MQERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKLEDVMAKLE 182
Cdd:COG3206 162 LEQNLELRREEARKALEFLE---EQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 183 EEKKKTNELEEELSAEKRRSTEMEA-----QMEKQLSEFDTEREQLRAKLNreEAHTT--DLKEEIDKMRKMIEQLKR 253
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYT--PNHPDviALRAQIAALRAQLQQEAQ 312
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-208 |
9.74e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 10 KKEFDVDTLSKS--ELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRfnLNDPFLALQRDYEagaGDKEKKpvct 87
Cdd:TIGR02169 333 KLLAEIEELEREieEERKRRDKLTEEYAELKEELEDLRAELEEV--DKEFAE--TRDELKDYREKLE---KLKREI---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 88 NPLsileavmahcKKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHKKLAARLEEERgknkqvvlmlvKECKQLSGKV 167
Cdd:TIGR02169 402 NEL----------KRELDRLQEELQRLSEELADLNAA---IAGIEAKINELEEEKEDKA-----------LEIKKQEWKL 457
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390010537 168 IEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQ 208
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
118-252 |
9.80e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 45.05 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEM--EKLQLQAL--EQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKVIEEAqklEDVMAKLEEEKKKTNELEE 193
Cdd:pfam05010 3 QKDMDAalEKARNEIEekELEINELKAKYEELRRENLEM------------RKIVAEF---EKTIAQMIEEKQKQKELEH 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 194 elsaekrrstemeAQMEKQLSEfdteREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:pfam05010 68 -------------AEIQKVLEE----KDQALADLNSVEKSFSDLFKRYEKQKEVISGYK 109
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
81-248 |
1.05e-04 |
|
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: 47.09 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 81 EKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEklqLQALEQ--EHKKLAA-RLEEERGKNKQV---VL 154
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQqlEEKAAAYdKLEKTKNRLQQElddLL 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 155 MLVKECKQLSGKvIEEAQKLEDVMakLEEEKKKTNELeeelsAEKRRSTEMEAQmekqlsefdtEREQLRAKLNREEAHT 234
Cdd:pfam01576 587 VDLDHQRQLVSN-LEKKQKKFDQM--LAEEKAISARY-----AEERDRAEAEAR----------EKETRALSLARALEEA 648
|
170
....*....|....
gi 1390010537 235 TDLKEEIDKMRKMI 248
Cdd:pfam01576 649 LEAKEELERTNKQL 662
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
725-757 |
1.12e-04 |
|
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: 40.74 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|....
gi 1390010537 725 DGHSALYSAA-KNGHTDCVRLLLSAEAQVNAADK 757
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
93-208 |
1.13e-04 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 43.84 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAES-RQKKLEMEKLQLQALE-QEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEE 170
Cdd:TIGR02473 22 LAKAQAEFERLETQLQQLIKYREEyEQQALEKVGAGTSALElSNYQRFIRQLDQRIQQQQQELALLQQEVEAKRERLLEA 101
|
90 100 110
....*....|....*....|....*....|....*...
gi 1390010537 171 AQKLEdVMAKLEEeKKKTNELEEELSAEKRRSTEMEAQ 208
Cdd:TIGR02473 102 RRELK-ALEKLKE-KKQKEYRAEEAKREQKEMDELATQ 137
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
91-232 |
1.18e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 91 SILEAVMA-------HCKKMQERMSAQLAAAESRQKKLEM---EKLQLQALEQEHKKlaaRLEEERGKNKQVVLMLVKEC 160
Cdd:PRK09510 48 SVIDAVMVdpgavveQYNRQQQQQKSAKRAEEQRKKKEQQqaeELQQKQAAEQERLK---QLEKERLAAQEQKKQAEEAA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 161 KQ--LSGKVIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRAKLNREEA 232
Cdd:PRK09510 125 KQaaLKQKQAEEAAAkaAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAAKAAAEA 199
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
695-837 |
1.22e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.59 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 695 LLQQAAAQGNVTLLSMLLNEEGLD-------------INYSCEDGHSALYSAAKNGHTDCVRLLLSAEAQVNAADKNGFT 761
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDerfveellhrgysPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 762 PL--CAAAAQGHFECVELLISYDANINHAAD-GGQTPLyLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGN 837
Cdd:PHA02946 108 PLyyLSGTDDEVIERINLLVQYGAKINNSVDeEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
114-256 |
1.24e-04 |
|
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs and only contains eukaryotic proteins. LUC7 has been shown to be a U1 snRNA associated protein with a role in splice site recognition. The family also contains human and mouse LUC7 like (LUC7L) proteins and human cisplatin resistance-associated overexpressed protein (CROP).
Pssm-ID: 460842 [Multi-domain] Cd Length: 246 Bit Score: 45.67 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 114 AESRQKKLEMEKLQLQALEQEHKKLAARLEE--ERGKnkqvvlmlvkeckqlsgkvIEEAQKLedvMAKLEEEKKKTNEL 191
Cdd:pfam03194 111 QEEIEQTDELKQEQISVLEEKIKKLLEEAEElgEEGN-------------------VDEAQKL---MKKVEELKEEKEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 192 EEEL-SAEKRRSTEMEAQME------KQLSEFDTERE--------------QLRAKLNReeahttdLKEEIDKmRKMIEQ 250
Cdd:pfam03194 169 EQQYeSLTKESAASQEKKMEvcevcgAFLIVNDADRRladhltgkqhlgyaKIRDTLEE-------LKEKIEE-RREERE 240
|
....*.
gi 1390010537 251 LKRGSD 256
Cdd:pfam03194 241 ERREKR 246
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
247-626 |
1.25e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 247 MIEQLKRGSDSKPSlslPRKTKDRRLVSISVGTEGTVTRSVACQTDlVTENADHMKKLPLTMPVKPSTGSP-LVSANAK- 324
Cdd:PHA03307 10 LIEAAAEGGEFFPR---PPATPGDAADDLLSGSQGQLVSDSAELAA-VTVVAGAAACDRFEPPTGPPPGPGtEAPANESr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 325 ------GSVCTSATMARPGIDRQASYGDLIG---ASVPAFPPPSANKI---------EENGPSTGSTPDPTSSTPPLPSN 386
Cdd:PHA03307 86 stptwsLSTLAPASPAREGSPTPPGPSSPDPpppTPPPASPPPSPAPDlsemlrpvgSPGPPPAASPPAAGASPAAVASD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 387 AA--------------------PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPG-LNPRIQAARFRF--------QGN 437
Cdd:PHA03307 166 AAssrqaalplsspeetarapsSPPAEPPPSTPPAAASPRPPRRSSPISASASSPApAPGRSAADDAGAsssdssssESS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 438 ANDPDQNGNTTQSPPSRDVSPTSRDNLVAkqlARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSLKTHGVA 517
Cdd:PHA03307 246 GCGWGPENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 518 RVDRGNPPPIPPKKPGLSQTPSPPH--------PQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQGNR-VINEENLPKS 588
Cdd:PHA03307 323 ESSSSSTSSSSESSRGAAVSPGPSPsrspspsrPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARaAVAGRARRRD 402
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1390010537 589 SSPQLP-----PKPSIDLTVAPAGCAVSALATSQVGAWPAATP 626
Cdd:PHA03307 403 ATGRFPagrprPSPLDAGAASGAFYARYPLLTPSGEPWPGSPP 445
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
27-250 |
1.28e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 27 LSVMEGELEARDLVIEAL--------RARRKEVfiqERYGRFN--LNDPFLALQRDY---EAGAGD-KE----------K 82
Cdd:pfam10174 438 LTTLEEALSEKERIIERLkeqreredRERLEEL---ESLKKENkdLKEKVSALQPELtekESSLIDlKEhasslassglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 83 KPVCTNPLSI-LEAVMAHCKKMQERMSAQLAAAESRQKKLEMeKLQLQALEQEhkklAARLEEERGKNKQVV---LMLVK 158
Cdd:pfam10174 515 KDSKLKSLEIaVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQE----VARYKEESGKAQAEVerlLGILR 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 159 EC---KQLSGKVIEEAQKLEDVMAKLE------------EEKKKTNELEEElsAEKRRSTEMEAQMEKQLSEFDTEREQL 223
Cdd:pfam10174 590 EVeneKNDKDKKIAELESLTLRQMKEQnkkvanikhgqqEMKKKGAQLLEE--ARRREDNLADNSQQLQLEELMGALEKT 667
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1390010537 224 RAKLN--------------REEAHTTDLKEEidkMRKMIEQ 250
Cdd:pfam10174 668 RQELDatkarlsstqqslaEKDGHLTNLRAE---RRKQLEE 705
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-253 |
1.39e-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: 46.30 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 152 VVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQM---EKQLSEFDTEREQLRAKLN 228
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaalARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*
gi 1390010537 229 REEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLR 111
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
19-258 |
1.61e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 19 SKSELRMLLSVMEGEleaRDLVIEALRarrkevfIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMA 98
Cdd:COG5185 115 SADILISLLYLYKSE---IVALKDELI-------KVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 99 HCKKMQErmsaqlaaaESRQKKLEMEKLQ-LQALEQEHKKLAARLEEERGKNKQVVlmlvKECKQLSGKVIEEAQKLEDV 177
Cdd:COG5185 185 TLGLLKG---------ISELKKAEPSGTVnSIKESETGNLGSESTLLEKAKEIINI----EEALKGFQDPESELEDLAQT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAKLEEEKKKTNELEEELSAEKR-RSTEMEAQMEKQLSEFDTEREQLRA--KLNREEAHTTDLKEEIDKMR--KMIEQLK 252
Cdd:COG5185 252 SDKLEKLVEQNTDLRLEKLGENAeSSKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAAEaeQELEESK 331
|
....*.
gi 1390010537 253 RGSDSK 258
Cdd:COG5185 332 RETETG 337
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
118-229 |
1.65e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 42.94 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKLQ--LQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEE-AQKLEDVMAKLEEEKKKTNELEEE 194
Cdd:pfam13863 3 EKKREMFLVQlaLDAKREEIERLEELLKQREEELEKKEQEL-KEDLIKFDKFLKEnDAKRRRALKKAEEETKLKKEKEKE 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1390010537 195 LsaekrrstemeAQMEKQLSEFDTEREQLRAKLNR 229
Cdd:pfam13863 82 I-----------KKLTAQIEELKSEISKLEEKLEE 105
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
8-230 |
1.68e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDvdtlskSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAgDKEKKPVCT 87
Cdd:COG5185 329 ESKRETE------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEEL-DSFKDTIES 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 88 NPLSILEAVMAHCKKMQErmsaqLAAAESRQKKlemeklqlqALEQEHKKLAARLEEERGKNKQVvlmlvkeckqlsGKV 167
Cdd:COG5185 389 TKESLDEIPQNQRGYAQE-----ILATLEDTLK---------AADRQIEELQRQIEQATSSNEEV------------SKL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 168 IEEAQK-LEDVMAKLEEEKK-----KTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNRE 230
Cdd:COG5185 443 LNELISeLNKVMREADEESQsrleeAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
111-276 |
1.77e-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: 45.91 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 111 LAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE 190
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 191 LEEELSAEKRRSTEMEAQMEKQL----------------------------------SEFDTER-EQLRAKLNREEAHTT 235
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylkylAPARREQaEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1390010537 236 DLKEEIDKMRKMIEQLKRgsdSKPSLSLPRKTKDRRLVSIS 276
Cdd:COG4942 168 ELEAERAELEALLAELEE---ERAALEALKAERQKLLARLE 205
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
169-252 |
1.78e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.60 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 169 EEAQK----LEDVMAKLEEEKKKTNEleeelsaEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEidKM 244
Cdd:pfam20492 2 EEAERekqeLEERLKQYEEETKKAQE-------ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES--AE 72
|
....*...
gi 1390010537 245 RKMIEQLK 252
Cdd:pfam20492 73 MEAEEKEQ 80
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
108-253 |
1.87e-04 |
|
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: 46.50 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 108 SAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKqvVLMLVKECKQLSGKVIEEAQKledVMAKLEEEKKK 187
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ--EIEKEEEKLAQVLKENKEEEK---EKKLQEEELKL 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 188 TNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
118-253 |
2.08e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.13 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKLQLQALEQEHKKLAARLEEErgkNKQvvlmLVKECKQLSGKVIEEAQKLE----DVMAkLEEEKKKTNELEE 193
Cdd:pfam13851 28 IKSLKEEIAELKKKEERNEKLMSEIQQE---NKR----LTEPLQKAQEEVEELRKQLEnyekDKQS-LKNLKARLKVLEK 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 194 ELSAEKRRSTEMEAQMEKqLSEfdtEREQLRAKLNR--EEAHT-TDLKEEI--DKMRKMIEQLKR 253
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEK-VER---ERDELYDKFEAaiQDVQQkTGLKNLLleKKLQALGETLEK 160
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
699-823 |
2.33e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 45.84 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 699 AAAQGNVTLLS-MLLNEEGLDINysCED--GHSALYSAAK-NGHTDCVRLLLSAEAQVNAADKngftpLCAAAAQGHFEC 774
Cdd:TIGR00870 24 AAERGDLASVYrDLEEPKKLNIN--CPDrlGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDA 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 775 VELLISY-------DANINHAADG-------GQTPLYLACKNGNKECIKLLLEAGTNRSVKTT 823
Cdd:TIGR00870 97 VEAILLHllaafrkSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
763-845 |
2.90e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.37 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 763 LCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNVDSLK 842
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
...
gi 1390010537 843 LLM 845
Cdd:PHA02875 86 ELL 88
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-263 |
2.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 116 SRQKKLEMEKLQLQALEQEHKKLAARLE--EERGKNKQVVLMLVKECKQLS------GKVIEEAQKLEDVMAKLEEEKKK 187
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 188 TNELEEELsaekrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSL 263
Cdd:COG4913 687 LAALEEQL-----------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
109-246 |
2.94e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSgkvIEEAQKLEDVMA----KLEEE 184
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAK---AEAEQRAAELAAeaakKLAEA 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 185 KKKTNELEEELSAEKRRStemEAQMEKQLSEfdtEREQLRAklnrEEAHTTDLKEEIDKMRK 246
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKA---AKEAEAAAAA---EKAAAAA----EKEKAEEAKRKAEEEAK 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-272 |
3.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 123 MEKLQLQA-LEQEHKKLAARLEEERgknkqvvlmlvkecKQLSGKVIEEaqkLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:TIGR02168 202 LKSLERQAeKAERYKELKAELRELE--------------LALLVLRLEE---LREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 202 StemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI----EQLKRGSDSKPSLSLPRKTKDRRL 272
Cdd:TIGR02168 265 L-------EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEELEAQLEELESKL 332
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
101-263 |
3.06e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---RLEEERGKNKQVVlmlvkecKQLSGKVIEEAQKLEDV 177
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQI-------AELQSEIAEREEELKEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAKLEEEKKKTNELEEELSAEKRRSTemEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRGSDS 257
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEA--EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
....*.
gi 1390010537 258 KPSLSL 263
Cdd:COG4372 234 ALSALL 239
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
149-250 |
3.23e-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: 42.56 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 149 NKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE-KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKL 227
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKElQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
90 100
....*....|....*....|....
gi 1390010537 228 NREEAhttDLKEEI-DKMRKMIEQ 250
Cdd:pfam03938 86 QKKQQ---ELLQPIqDKINKAIKE 106
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
117-232 |
3.26e-04 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 42.69 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 117 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE----KKKTNELE 192
Cdd:TIGR02473 11 REKEEEQAKLELAKAQAEFERLETQLQQLIKYREE--YEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqQQELALLQ 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1390010537 193 EELsaEKRRSTEMEAQMEKQLseFDTEREQLRAKLNREEA 232
Cdd:TIGR02473 89 QEV--EAKRERLLEARRELKA--LEKLKEKKQKEYRAEEA 124
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
76-232 |
3.26e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.84 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 76 GAGDKEKKPVCTNPLSILEAVMAHCKKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLM 155
Cdd:TIGR02794 21 GSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 156 LVKECKQlsgkvIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:TIGR02794 100 AEKAAKQ-----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-257 |
3.28e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 35 EARDLVIEALRARRkevFIQERYGRFNLNDPFLA-----------LQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCK-- 101
Cdd:PRK04863 898 EIREQLDEAEEAKR---FVQQHGNALAQLEPIVSvlqsdpeqfeqLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSye 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 102 KMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergkNKQVVLMLVKECKQLSGKVIEEAQKLED--VMA 179
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQ----YNQVLASLKSSYDAKRQMLQELKQELQDlgVPA 1050
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 180 KLEEEKKkTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEahttdlkEEIDKMRKMIEQLKRGSDS 257
Cdd:PRK04863 1051 DSGAEER-ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE-------RDYHEMREQVVNAKAGWCA 1120
|
|
| MFAP1 |
pfam06991 |
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with ... |
169-270 |
3.88e-04 |
|
Microfibril-associated/Pre-mRNA processing; MFAP1 was first named for proteins associated with microfibrils which are an important component of the extracellular matrix (ECM) of many tissues. For example, MFAP1 has been shown to be associated with elastin-like fibres at the base of Schlemm's canal endothelium cells, in the juxtacanalicular tissue, and in the uveal region. Based on its role in the ECM and the proximity of the MFAP1 gene to FBN1 it was hypothesized that mutations in MFAP1 contributed to heritable diseases affecting microfibrils, Marfan syndrome but this has now been shown not to be the case. MFAP1 has also been shown to interact directly with certain pre-mRNA processing factor proteins, Prps, which are also spliceosome components and is thus required for pre-mRNA processing. MAFP1 bound to Pr38 of yeast is necessary for cells in vivo to progress from G2 to M phase.
Pssm-ID: 462060 [Multi-domain] Cd Length: 215 Bit Score: 43.70 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 169 EEAQKLEDVMAKLEEEKKKTNEL-EEELsaeKRRSTEMEAQMEKQ-LSEFDTE--------------REQLRAKLNREEA 232
Cdd:pfam06991 34 EEEEEEEEAKKEAEERKKEADKLvEEEI---RREAAAKEAGDEDEnEEDVDDTdgldpeaeyeawklRELKRIKRDREER 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 1390010537 233 HTTD-LKEEIDKMRKMIEQLKRGSDSKpslsLPRKTKDR 270
Cdd:pfam06991 111 EAREkEREEIERRRNMTEEERLAEDRE----NPKKQREK 145
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
151-246 |
3.92e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 42.75 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 151 QVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTE---MEAQMEKQLSEfdTEREQLRAKL 227
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEearRKKEEEKELKE--KERREKKEKD 78
|
90
....*....|....*....
gi 1390010537 228 NREEAHTTDLKEEIDKMRK 246
Cdd:pfam11600 79 EKEKAEKLRLKEEKRKEKQ 97
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
792-822 |
4.01e-04 |
|
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: 39.19 E-value: 4.01e-04
10 20 30
....*....|....*....|....*....|..
gi 1390010537 792 GQTPLYLAC-KNGNKECIKLLLEAGTNRSVKT 822
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
825-914 |
4.01e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 825 GWTPVHAAVDTGNVDSLKLLMYHRIPahgnsfneeesessvfdldggeespegiskpvvpadlINHANREGWTAAHIAAS 904
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD-------------------------------------INAVDGNGETALHFAAS 43
|
90
....*....|
gi 1390010537 905 KGFKNCLEIL 914
Cdd:pfam13637 44 NGNVEVLKLL 53
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
101-260 |
4.09e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERM-SAQLAAAeSRQKKLEMEKLQLQALE-QEHKKLAAR---LEEERGKNkqvvlmlVKECKQLSGKVIEEAQKLE 175
Cdd:PRK11637 119 QAAQERLlAAQLDAA-FRQGEHTGLQLILSGEEsQRGERILAYfgyLNQARQET-------IAELKQTREELAAQKAELE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 176 DVMAK----LEEEKKKTNELEEELSAEKRRSTEMEAQMEK---QLSEFDTEREQLRAKLNREEAHTTDLKE----EIDKM 244
Cdd:PRK11637 191 EKQSQqktlLYEQQAQQQKLEQARNERKKTLTGLESSLQKdqqQLSELRANESRLRDSIARAEREAKARAErearEAARV 270
|
170
....*....|....*..
gi 1390010537 245 RKMIEQLKR-GSDSKPS 260
Cdd:PRK11637 271 RDKQKQAKRkGSTYKPT 287
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
109-228 |
4.11e-04 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 41.05 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLaarLEEergknkqvvLMLVKE---CKQLSGKVIEEaQKLEDVMAKLEEEK 185
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELA---LEE---------LELLDEdtkVYKLIGDVLVK-QDKEEVKEQLEERK 68
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1390010537 186 KKtneLEEELSAekrrstemeaqMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam01920 69 ET---LEKEIKT-----------LEKQLEKLEKELEELKEELY 97
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
305-497 |
4.11e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 45.25 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 305 PLTMPVKP-STGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPS----ANKIEENGPSTGSTPDPTSS 379
Cdd:PRK12323 374 PATAAAAPvAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealAAARQASARGPGGAPAPAPA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 380 TPPLPSNAAPPTAQTPGIAPQNSQAPPmhSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPDQNGnttqsPPSRDVSPT 459
Cdd:PRK12323 454 PAAAPAAAARPAAAGPRPVAAAAAAAP--ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA-----PAGWVAESI 526
|
170 180 190
....*....|....*....|....*....|....*...
gi 1390010537 460 SRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPT 497
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPR 564
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
104-228 |
4.21e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.86 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAARLEE--ERgknkQVVlmlvkeckqlsgKVIEEAQKLEDVMAKL 181
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyER----ELV------------LHAEDIKALQALREEL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1390010537 182 EEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRIE 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
94-252 |
4.28e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 94 EAVMAHCKkmqERMSAQLAAAES------RQKKLEMEKL------QLQALEQEHKKLA--ARLEEERgknkqvvlmLVKE 159
Cdd:NF041483 282 EKVVAEAK---EAAAKQLASAESaneqrtRTAKEEIARLvgeatkEAEALKAEAEQALadARAEAEK---------LVAE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 160 CKQLSGKVIEE---------AQKLEDVMAKLEEEKKKTNELEEElSAEKRRsTEMEAQMEKQLSEFDTEREQLR--AKLN 228
Cdd:NF041483 350 AAEKARTVAAEdtaaqlakaARTAEEVLTKASEDAKATTRAAAE-EAERIR-REAEAEADRLRGEAADQAEQLKgaAKDD 427
|
170 180
....*....|....*....|....*.
gi 1390010537 229 REE--AHTTDLKEEIDKMRKMIEQLK 252
Cdd:NF041483 428 TKEyrAKTVELQEEARRLRGEAEQLR 453
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
107-253 |
4.34e-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: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 107 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVlMLVKEcKQLSGKviEEAQ-KLEDVMAKL 181
Cdd:pfam15619 58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 182 EEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLsefdtereQLRAKLNreeahttDLKEEIDKMRKMIEQLKR 253
Cdd:pfam15619 134 EDKDEKIQDLERKLElENKSFRRQLAAEKKKHK--------EAQEEVK-------ILQEEIERLQQKLKEKER 191
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
122-253 |
4.37e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 122 EMEKLQLQALEQEHKKLaarleeeRGKNKQVVLMLVKECKQLSgkvieEAQKLEDVMAKLEEEKKKTNELEEELSAEKRR 201
Cdd:PRK00106 31 EAAELTLLNAEQEAVNL-------RGKAERDAEHIKKTAKRES-----KALKKELLLEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 202 STEMEAQMEKQLSEFDTEREQLRAK---LNREEAHTTDLKEEIDKMRKMIEQLKR 253
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKektLESKEQSLTDKSKHIDEREEQVEKLEE 153
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
139-269 |
4.55e-04 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 42.48 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 139 AARLEE-ERGKNKQVvlmlvkECKQLSGKVIEEAQKLEdvmaKLEEEKKKTNELEEELsaEKRRSTEMeaqMEKQLsefd 217
Cdd:pfam15236 41 PAQLEErERKRQKAL------EHQNAIKKQLEEKERQK----KLEEERRRQEEQEEEE--RLRREREE---EQKQF---- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 218 tEREQLRAKlNREEAHTTDLKEEIDKMRKMIEQLKRGSDSKPSLSLPRKTKD 269
Cdd:pfam15236 102 -EEERRKQK-EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIRELAEKGHD 151
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
98-281 |
4.56e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 98 AHCKKMQERMSAQLAAAESRQKKLEmeklqlqaLEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKL--- 174
Cdd:COG3064 39 AEEERLAELEAKRQAEEEAREAKAE--------AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAaaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 --EDVMAKLE--EEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:COG3064 111 ekAAAAAEKEkaEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
|
170 180 190
....*....|....*....|....*....|.
gi 1390010537 251 LKRGSDSKPSLSLPRKTKDRRLVSISVGTEG 281
Cdd:COG3064 191 EAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-230 |
4.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEE 183
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 184 EKKKTNELE--------------EELSAEKRRSTEMEAQMEKqLSEfdtEREQLR---AKLNRE 230
Cdd:COG1196 765 LERELERLEreiealgpvnllaiEEYEELEERYDFLSEQRED-LEE---ARETLEeaiEEIDRE 824
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
312-693 |
4.94e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 312 PSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPT 391
Cdd:PHA03307 49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 392 AQTPGIAPqnsQAPPMHSLHSPCANTSLHPGLNPRIQAArfrfqgNANDPDQNGNTTQSPPS--RDVSPTSRDNLVAKQL 469
Cdd:PHA03307 129 SPAPDLSE---MLRPVGSPGPPPAASPPAAGASPAAVAS------DAASSRQAALPLSSPEEtaRAPSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 470 ARntvtqalsrfTSPQAGAPSRPGVPPTGDVGTHPpvGRTSLKTHGVARVDRGNPPPIPPKKPGLSQTPSPPHPQlkviI 549
Cdd:PHA03307 200 AA----------ASPRPPRRSSPISASASSPAPAP--GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP----I 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 550 DSSRASNTGAKVDNKTVASTPSSLPQGNRVINEENLP-KSSSPQLPPKPSIDLTVAPAGCAVSA--LATSQVGAWPAATP 626
Cdd:PHA03307 264 TLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPsSPGSGPAPSSPRASSSSSSSRESSSSstSSSSESSRGAAVSP 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1390010537 627 GlnQPACSDSSLVIPTTIAFCSS----INPVSASSCRPGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRP 693
Cdd:PHA03307 344 G--PSPSRSPSPSRPPPPADPSSprkrPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRP 412
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-244 |
5.09e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 184
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 185 KKKTNELEEELSAEkrrstEMEAQMEKQLSEFDteREQLRAKLNReeahttdLKEEIDKM 244
Cdd:COG1196 734 REELLEELLEEEEL-----LEEEALEELPEPPD--LEELERELER-------LEREIEAL 779
|
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
103-229 |
5.12e-04 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 41.41 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 103 MQERMSAQLaaaesrQKKLEmeklQLQALEQEHKKLAARleeergknKQVVLMLVKECKqlsgKVIEEAQKLED------ 176
Cdd:COG1382 1 MMQNLPPEV------QNQLA----QLQQLQQQLQAVAAQ--------KQQVESELKEAE----KALEELEKLPDdaevyk 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 177 ----VMAKLEEEKKKtNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNR 229
Cdd:COG1382 59 svgnLLVKTDKEEVI-KELEEKKETLELRLKTLEKQEERLQKQLEELQEKLQEALSG 114
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-252 |
5.24e-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: 45.04 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 18 LSKSElRMLLSVMEGELEARDL-----VIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvcTNPLSI 92
Cdd:TIGR00606 767 IEEQE-TLLGTIMPEEESAKVCltdvtIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEK---QHELDT 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEergKNKQVvLMLVKECKQLSGKVIEEAQ 172
Cdd:TIGR00606 841 VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE---LSTEV-QSLIREIKDAKEQDSPLET 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLED-------VMAKLEEEKK----KTNELEEELSAE--KRRSTEMEAQ--MEKQLSEFDTEREQLRAKLNREEAHTTDL 237
Cdd:TIGR00606 917 FLEKdqqekeeLISSKETSNKkaqdKVNDIKEKVKNIhgYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKI 996
|
250
....*....|....*
gi 1390010537 238 KEEIDKMRKMIEQLK 252
Cdd:TIGR00606 997 NEDMRLMRQDIDTQK 1011
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
117-229 |
5.30e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.72 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 117 RQKKLEMEKLQLQALEQEhkklAARLEEERGKNKQVvlmlvkeckqlsgkvIEEAQK-----LEDVMAKLEEEKKKTNEL 191
Cdd:cd16269 196 KEKEIEAERAKAEAAEQE----RKLLEEQQRELEQK---------------LEDQERsyeehLRQLKEKMEEERENLLKE 256
|
90 100 110
....*....|....*....|....*....|....*...
gi 1390010537 192 EEELSAEKRRstEMEAQMEKqlsEFDTEREQLRAKLNR 229
Cdd:cd16269 257 QERALESKLK--EQEALLEE---GFKEQAELLQEEIRS 289
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
109-198 |
5.67e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 41.23 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 109 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECKQLSGKVIEEAQK-------LEDVM 178
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQKekekqseLDDLL 80
|
90 100
....*....|....*....|....*..
gi 1390010537 179 -------AKLEEEKKKTNELEEELSAE 198
Cdd:pfam04871 81 lllgdleEKVEKYKARLKELGEEVLSD 107
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
305-499 |
5.92e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 305 PLTMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSAnkieengPSTGSTPDPTSSTPPLP 384
Cdd:PRK12323 402 PPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAA-------PAAAARPAAAGPRPVAA 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 385 SNAAPPTAQTPGI--APQNSQAPPMHSLHSPCANTSLHPglnpriQAARFRFQGNANDPDQngNTTQSPPSRdvsPTSRD 462
Cdd:PRK12323 475 AAAAAPARAAPAAapAPADDDPPPWEELPPEFASPAPAQ------PDAAPAGWVAESIPDP--ATADPDDAF---ETLAP 543
|
170 180 190
....*....|....*....|....*....|....*..
gi 1390010537 463 NLVAKQLARntVTQALSRFTSPQAGAPSRPGVPPTGD 499
Cdd:PRK12323 544 APAAAPAPR--AAAATEPVVAPRPPRASASGLPDMFD 578
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
114-252 |
6.11e-04 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 42.72 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 114 AESRQKKLeMEKLQLQALEQ-------EHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEaqkLEDVMAKLEEEKK 186
Cdd:pfam15035 10 AQQRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLEREHSAD---LEEALIRLEEERQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 187 KTNEL-----------EEELSAEKRRSTEMEA----------QMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam15035 86 RSESLsqvnsllreqlEQASRANEALREDLQKltndwerareELEQKESEWRKEEEAFNEYLSSEHSRLLSLWREVVAVR 165
|
....*..
gi 1390010537 246 KMIEQLK 252
Cdd:pfam15035 166 RQFTELK 172
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
257-508 |
6.47e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.78 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 257 SKPSLSLPRKTKDRRLVSISVGTEgtvTRSVACQTDLVTENADHMKKlPLTMPVKPSTGSPlvsANAKGSVCTSATMARP 336
Cdd:PHA03307 218 SSPAPAPGRSAADDAGASSSDSSS---SESSGCGWGPENECPLPRPA-PITLPTRIWEASG---WNGPSSRPGPASSSSS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 337 GIDRQASYGDlIGASVPAFPPPSANKiEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSLHSPCAN 416
Cdd:PHA03307 291 PRERSPSPSP-SSPGSGPAPSSPRAS-SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 417 TSLHPGL-NPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTvtqalsrFTSPQAGAPSR---P 492
Cdd:PHA03307 369 PRPSRAPsSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAF-------YARYPLLTPSGepwP 441
|
250
....*....|....*.
gi 1390010537 493 GVPPtgdvgthPPVGR 508
Cdd:PHA03307 442 GSPP-------PPPGR 450
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
772-838 |
7.05e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 44.22 E-value: 7.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 772 FECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVDTGNV 838
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
105-245 |
7.37e-04 |
|
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: 44.13 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEE 184
Cdd:pfam15964 548 NEAKAQALQAQQREQELTQ---KMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQE 624
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 185 KKKTNELEEELsaeKRRSTEMEAQ----------MEKQLSEFD----TEREQLRAKLNREEA---HTTDLKEEIDKMR 245
Cdd:pfam15964 625 KEYLQDRLEKL---QKRNEELEEQcvqhgrmherMKQRLRQLDkhcqATAQQLVQLLSKQNQlfkERQNLTEEVQSLR 699
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
725-754 |
7.41e-04 |
|
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: 38.34 E-value: 7.41e-04
10 20 30
....*....|....*....|....*....|
gi 1390010537 725 DGHSALYSAAKNGHTDCVRLLLSAEAQVNA 754
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| DUF874 |
pfam05917 |
Helicobacter pylori protein of unknown function (DUF874); This family consists of several ... |
107-233 |
7.43e-04 |
|
Helicobacter pylori protein of unknown function (DUF874); This family consists of several hypothetical proteins specific to Helicobacter pylori. The function of this family is unknown.
Pssm-ID: 283549 [Multi-domain] Cd Length: 398 Bit Score: 44.07 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 107 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQvvlmlvkeckqlSGKVIEEAQ-KLEDVMAKLEEEK 185
Cdd:pfam05917 115 LAACSAGDTDEQIELEQEKKEAENAEDRANKNGIELEQEKQKTNK------------SGIELANNQiKAEQEQQKTEQEK 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1390010537 186 KKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQlraklNREEAH 233
Cdd:pfam05917 183 QKAEKEAIELEQEKQKTIKTQRDLIKEQKDFIKETEQ-----NCQENH 225
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
22-253 |
7.62e-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: 44.35 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARDlviEALRARRKEVFIQERYgrfnlNDPFLALQRDYEAGAGD-KEKKPVCTNPLSILeAVMAHC 100
Cdd:pfam05557 52 ELQKRIRLLEKREAEAE---EALREQAELNRLKKKY-----LEALNKKLNEKESQLADaREVISCLKNELSEL-RRQIQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQerMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQK------- 173
Cdd:pfam05557 123 AELE--LQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKselarip 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 -LEDVMAKLEEEKKKTNE-------LEEELSAEKRRSTEMEAQMEKqLSEFDTEREQLRAKLNR----EEAHTTDLKEEI 241
Cdd:pfam05557 201 eLEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSwvklAQDTGLNLRSPE 279
|
250
....*....|..
gi 1390010537 242 DKMRKMIEQLKR 253
Cdd:pfam05557 280 DLSRRIEQLQQR 291
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
699-938 |
8.01e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 699 AAAQGNVTLLSMLLNeegldINYSCEDGHSALYSAAKNghTDCVRLLLSAEaqVNAADKNGFTPLCAAAAQGHFECVELL 778
Cdd:cd22194 90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 779 ISYDANINHAADG--------------GQTPLYLACKNGNKECIKLLLEAG-TNRSVKTTDGWTPVHAAV----DTGNVD 839
Cdd:cd22194 161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 840 SLKLLMYHRIPahgnsfneeesessvfdLDGGEESPEGISkpvvpadlinhaNREGWTAAHIAASKGfknCLEILcrHGG 919
Cdd:cd22194 241 DFVKRMYDMIL-----------------LKSENKNLETIR------------NNEGLTPLQLAAKMG---KAEIL--KYI 286
|
250
....*....|....*....
gi 1390010537 920 LEPERRDKCNRTVHDVATD 938
Cdd:cd22194 287 LSREIKEKPNRSLSRKFTD 305
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
124-250 |
8.16e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 124 EKLQLQALEQEHKKLAARLEEERGKNKQvvlmLVKECKQLSgkvieEAQKLEDVMAKLE-EEKKKTNELEEElsaekRRS 202
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAE----AEQKAKEEA-----EEERLAELEAKRQaEEEAREAKAEAE-----QRA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1390010537 203 TEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:COG3064 69 AELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAA 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
127-254 |
8.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 127 QLQALEQEHKKLAARLEEERgknkqvvlmLVKECKQLSGKV----IEEAQKLEDVMAKLEEEKKKTNELEEEL-SAEKRR 201
Cdd:COG4717 348 ELQELLREAEELEEELQLEE---------LEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLeELLGEL 418
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 202 STEMEAQMEKQLSEfdtEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG4717 419 EELLEALDEEELEE---ELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
94-248 |
8.65e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.09 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 94 EAVMAHCKKMQERMSAQL-------AAAESRQKKLEMEKlQLQALEQEHKKLAARLEEErgknkqvVLMLVKECKQLSGK 166
Cdd:PRK00106 52 ERDAEHIKKTAKRESKALkkellleAKEEARKYREEIEQ-EFKSERQELKQIESRLTER-------ATSLDRKDENLSSK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 167 --VIEEA-QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:PRK00106 124 ekTLESKeQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILAETENKLTHEIATRIREAEREVKDRSDK 203
|
....*
gi 1390010537 244 MRKMI 248
Cdd:PRK00106 204 MAKDL 208
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
33-210 |
8.72e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 33 ELEARDLVIEAlrarRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKpvctnpLSILEAVMahcKKMQERMSAQLA 112
Cdd:PRK12704 37 EEEAKRILEEA----KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE------LQKLEKRL---LQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 113 AAESRQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkeckqlsgKVIEEAQKLEDVMAKLEEEKKKT--NE 190
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEE---------------------LIEEQLQELERISGLTAEEAKEIllEK 162
|
170 180
....*....|....*....|...
gi 1390010537 191 LEEELSAEKR---RSTEMEAQME 210
Cdd:PRK12704 163 VEEEARHEAAvliKEIEEEAKEE 185
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
730-802 |
1.01e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.05 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 730 LYSAAKNGHtDCVRLLLSAEAQVNA-ADKNGFTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLA---CKN 802
Cdd:PHA02884 75 IYAIDCDND-DAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNN 150
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
305-504 |
1.03e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.90 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 305 PLTMPVKPSTGS--PLVSANAKGSVCTSATMARPGIDRQASYGDLIGASvPAFPPPSANKIEE----NGPSTGSTPDPTS 378
Cdd:PHA03378 602 PSQTPEPPTTQShiPETSAPRQWPMPLRPIPMRPLRMQPITFNVLVFPT-PHQPPQVEITPYKptwtQIGHIPYQPSPTG 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 379 STPPLPSNAAPPTAQTPGIAPqnSQAPPMHSLHSPCANTSLHPGLNPRIQAARFRFQGNANDPdqngntTQSPPSRDVSP 458
Cdd:PHA03378 681 ANTMLPIQWAPGTMQPPPRAP--TPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAP------GRARPPAAAPG 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1390010537 459 TSRDNLVAKQLARntvtqalsrftsPQAGAPSRPGVPPTGDVGTHP 504
Cdd:PHA03378 753 RARPPAAAPGRAR------------PPAAAPGAPTPQPPPQAPPAP 786
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
94-250 |
1.03e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.43 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 94 EAVMAHCKKMQERMSAQLAAAESRQKKLEmEKLQLQALEQEHKKLAARLEEergknkqvvlmlvKECKQLSGKVIEEAQK 173
Cdd:cd00176 75 EEIQERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEE-------------KEAALASEDLGKDLES 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTER-EQLRAKLNReeahttdLKEEIDKMRKMIEQ 250
Cdd:cd00176 141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKlEELNERWEE-------LLELAEERQKKLEE 211
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
105-324 |
1.03e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQV---VLMLVKECkqlsgKVIEEAQKLEDVMAKL 181
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAkkrFSLLKKET-----IYLQSAQRVELAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 182 EEEKK----------KTNELEEELSaEKRRS------------TEMEAQMEKQLSEFDTEREQLR--------AKLNREE 231
Cdd:COG5022 885 QELKIdvksisslklVNLELESEII-ELKKSlssdlienlefkTELIARLKKLLNNIDLEEGPSIeyvklpelNKLHEVE 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 232 AHTTDLKEEIDKMRKMIEQLKRgsDSKPSLSLPRKTKdRRLVSISvgtegtvtrsvaCQTDLVTENADHMKKLPLTMPVK 311
Cdd:COG5022 964 SKLKETSEEYEDLLKKSTILVR--EGNKANSELKNFK-KELAELS------------KQYGALQESTKQLKELPVEVAEL 1028
|
250
....*....|...
gi 1390010537 312 PSTGSPLVSANAK 324
Cdd:COG5022 1029 QSASKIISSESTE 1041
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
103-253 |
1.03e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 103 MQERMSAQLAAAESRQKKLEMEKLQLQAlEQE--HKKLAARLEEERGKNKqvvlmlvkeckqlsgkvieeaQKLEDVMAK 180
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKK-EQDeaSFERLAELRDELAELE---------------------EELEALKAR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 181 LEEEKKKTNE---LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREE-----AHTTD------LKEEIDKMRK 246
Cdd:COG0542 463 WEAEKELIEEiqeLKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvSRWTGipvgklLEGEREKLLN 542
|
....*..
gi 1390010537 247 MIEQLKR 253
Cdd:COG0542 543 LEEELHE 549
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
117-461 |
1.04e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 117 RQKKLEMEKLQLQALEQEHKKLAARLEEE---RGKNKQVvlmLVKECKQLSGKVIEEAQ--KLEDVMAKLEEEKKKTNEL 191
Cdd:PTZ00108 997 KEYLLGKLERELARLSNKVRFIKHVINGElviTNAKKKD---LVKELKKLGYVRFKDIIkkKSEKITAEEEEGAEEDDEA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 192 EEELSAEKRRST----------------EMEAQMEKQLSEFDTEREQLRAKlNREEAHTTDLK---EEIDKMRKMIEQLK 252
Cdd:PTZ00108 1074 DDEDDEEELGAAvsydyllsmpiwsltkEKVEKLNAELEKKEKELEKLKNT-TPKDMWLEDLDkfeEALEEQEEVEEKEI 1152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 253 RGSDSKPSlslPRKTKDRRLVSisvgtegtvtrsvacQTDLVTENADHMKKLPLTMPVKPSTGSPLVSANAKGSVCTSAT 332
Cdd:PTZ00108 1153 AKEQRLKS---KTKGKASKLRK---------------PKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPD 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 333 MARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMHSL-- 410
Cdd:PTZ00108 1215 NKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPdg 1294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 411 ---HSPCANTSLHPGLNPRIQ----AARFRFQGNANDPDQNGNTTQSPPSRDVSPTSR 461
Cdd:PTZ00108 1295 esnGGSKPSSPTKKKVKKRLEgslaALKKKKKSEKKTARKKKSKTRVKQASASQSSRL 1352
|
|
| CCDC66 |
pfam15236 |
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ... |
104-194 |
1.04e-03 |
|
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.
Pssm-ID: 434558 [Multi-domain] Cd Length: 154 Bit Score: 41.32 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAEsRQKKLEMEK------LQLQALEQEHKKLAARLEEERGKNKQvvlmlVKECKQLSGKVIEEAQKLEDV 177
Cdd:pfam15236 58 QNAIKKQLEEKE-RQKKLEEERrrqeeqEEEERLRREREEEQKQFEEERRKQKE-----KEEAMTRKTQALLQAMQKAQE 131
|
90
....*....|....*..
gi 1390010537 178 MAKLEEEKKKTNELEEE 194
Cdd:pfam15236 132 LAQRLKQEQRIRELAEK 148
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
172-258 |
1.06e-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: 42.60 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELSAEKrrstemeAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRkmiEQL 251
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDEL-------AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQL 82
|
....*..
gi 1390010537 252 KRGSDSK 258
Cdd:COG1579 83 GNVRNNK 89
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
761-845 |
1.11e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 761 TPL--CAAAAQGHFECVELLISYDANINHAADG-GQTPL--YLAC-KNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAVD 834
Cdd:PHA02859 53 TPIfsCLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhYLSFnKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
|
90
....*....|...
gi 1390010537 835 TGNV--DSLKLLM 845
Cdd:PHA02859 133 NFNVriNVIKLLI 145
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
101-232 |
1.12e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMS--AQLAAAESRQKKLEMEKLQLQALEQEHKK-LAARLEEERGKNKQVVLMlvKECKQLS-GKVIEEAQKLE- 175
Cdd:pfam15709 372 EKMREELEleQQRRFEEIRLRKQRLEEERQRQEEEERKQrLQLQAAQERARQQQEEFR--RKLQELQrKKQQEEAERAEa 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 176 ------DVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA 232
Cdd:pfam15709 450 ekqrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
101-228 |
1.14e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESR-----QKKLEMEK-LQLQALEQEHKKLAARLE-EERGKNKQVVLMLVKECKQLSGKVIEEAQK 173
Cdd:pfam10473 2 EKKQLHVLEKLKESERKadslkDKVENLEReLEMSEENQELAILEAENSkAEVETLKAEIEEMAQNLRDLELDLVTLRSE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 174 LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLN 228
Cdd:pfam10473 82 KENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQTQLK 136
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
124-254 |
1.17e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 43.05 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 124 EKLQLQALEQEHKKLAARLEEERgknkqvvlmlvkeckqlsgkvIEEAQKLEDVMAKLEEEKKKT-----NELEEElsaE 198
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLER---------------------VLEKIAESAATAEAREEKRKTkaqrnKEKRRK---E 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 199 KRRSTEMEAQMEKQLSEFDTEREqLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:pfam07767 254 EEREAKEEKALKKKLAQLERLKE-IAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
112-243 |
1.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 112 AAAesrQKKLEMEKL--QLQALEQEHkklaARLEEERGKnkqvvlmLVKECKQLSgkvIEEAQKLEDVMAKLEEEKkktN 189
Cdd:COG0542 398 AAA---RVRMEIDSKpeELDELERRL----EQLEIEKEA-------LKKEQDEAS---FERLAELRDELAELEEEL---E 457
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 190 ELEEELSAEK---RRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:COG0542 458 ALKARWEAEKeliEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
177-253 |
1.21e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 40.93 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 177 VMAKLEEEKKK-TNELEEelsAEKRRS--TEMEAQMEKQLSEFDTEREQLRAKLNRE-----EAHTTDLKEEIDKMRKM- 247
Cdd:COG0711 25 ILKALDERQEKiADGLAE---AERAKEeaEAALAEYEEKLAEARAEAAEIIAEARKEaeaiaEEAKAEAEAEAERIIAQa 101
|
....*....
gi 1390010537 248 ---IEQLKR 253
Cdd:COG0711 102 eaeIEQERA 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
103-249 |
1.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 103 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLA-----ARLEEERG--KNKQVVLMLVKECKQLSGKVieeaQKLE 175
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDyfKYKNDIENKKQILSNIDAEI----NKYH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 176 DVMAKLEEEKKKTNELEEelsaEKRRSTEmeaqMEKQLSEFDT----------EREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:PRK01156 326 AIIKKLSVLQKDYNDYIK----KKSRYDD----LNNQILELEGyemdynsylkSIESLKKKIEEYSKNIERMSAFISEIL 397
|
....
gi 1390010537 246 KMIE 249
Cdd:PRK01156 398 KIQE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-270 |
1.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 117 RQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELs 196
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI-ERYEEQREQARETRDEADEVLEEHEERREELETLEAEI- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 197 aEKRRSTEMEAQMEK------------QLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG-SDSKPSLSL 263
Cdd:PRK02224 261 -EDLRETIAETEREReelaeevrdlreRLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQA 339
|
....*..
gi 1390010537 264 PRKTKDR 270
Cdd:PRK02224 340 HNEEAES 346
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
105-230 |
1.26e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.51 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLvkECKQLSGKVIEEaqKLEDVMAKLEEE 184
Cdd:pfam05911 698 ENLEVELASCT---ENLESTKSQLQESEQLIAELRSELASLKESNSLAETQL--KCMAESYEDLET--RLTELEAELNEL 770
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 185 KKKTNELEEELSAEKR-------RSTEMEAQME----KQLSEFDTEREQLRAKLNRE 230
Cdd:pfam05911 771 RQKFEALEVELEEEKNcheeleaKCLELQEQLErnekKESSNCDADQEDKKLQQEKE 827
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
91-253 |
1.30e-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: 43.63 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 91 SILEAVMAHCKKMQERMSA---------QLAAAESRQKkLEMEKlQLQALEQEHKKLAARLEEERGKNKQVVlmlvKECK 161
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSlesqlqdtqELLQEETRQK-LNLST-RLRQLEDERNSLQEQLEEEEEAKRNVE----RQLS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 162 QLSGKVIEEAQKLED---VMAKLEEEKKKtneLEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNreeahttDLK 238
Cdd:pfam01576 521 TLQAQLSDMKKKLEEdagTLEALEEGKKR---LQRELEALTQQLEEKAAAYDK----LEKTKNRLQQELD-------DLL 586
|
170
....*....|....*
gi 1390010537 239 EEIDKMRKMIEQLKR 253
Cdd:pfam01576 587 VDLDHQRQLVSNLEK 601
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
90-249 |
1.42e-03 |
|
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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 90 LSILEAVMAHCKKMQERMSAQLAAAESRQKKL---EMEKLQLQALEQEHKKLAARLEEERGKN---KQVVLMLVKE---C 160
Cdd:TIGR00606 600 LASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAMLAGATavySQFITQLTDEnqsC 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 161 KQLSGKVIEEAQKLEDVMAKLEEEKK----KTNELEEELSAEKRRSTEMEAQMEKQLSEFD---TEREQLRAKLNREEAH 233
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRD 759
|
170
....*....|....*.
gi 1390010537 234 TTDLKEEIDKMRKMIE 249
Cdd:TIGR00606 760 IQRLKNDIEEQETLLG 775
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
169-250 |
1.48e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 41.73 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 169 EEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam06785 87 ILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLESEEQLAEKQLLINEYQQTIEEQRSVL 166
|
..
gi 1390010537 249 EQ 250
Cdd:pfam06785 167 EK 168
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
166-253 |
1.52e-03 |
|
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: 40.64 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 166 KVIEEAQKLEDVMAKLEEEKKKtneleeelsaekrrsteMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMR 245
Cdd:pfam03938 9 KILEESPEGKAAQAQLEKKFKK-----------------RQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKE 71
|
....*...
gi 1390010537 246 KMIEQLKR 253
Cdd:pfam03938 72 QELQQLQQ 79
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
695-906 |
1.62e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 695 LLQQAAAQGNvtlLSMLLNEEGLDINYsceDGHSALYSAAKNGHTDCVRLLLSAEAQVNAAdkngftpLCAAAAQGHfec 774
Cdd:cd21882 48 LLEAAPDSGN---PKELVNAPCTDEFY---QGQTALHIAIENRNLNLVRLLVENGADVSAR-------ATGRFFRKS--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 775 VELLISYdaninhaadgGQTPLYLACKNGNKECIKLLLEAGTN-RSVKTTD--GWTPVHAAVDTGN--VDSLKLL--MYH 847
Cdd:cd21882 112 PGNLFYF----------GELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQADntPENSAFVcqMYN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 848 RIPAHGNSfneeesessvfdldggeespegiSKPVVPADLInhANREGWTAAHIAASKG 906
Cdd:cd21882 182 LLLSYGAH-----------------------LDPTQQLEEI--PNHQGLTPLKLAAVEG 215
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
104-253 |
1.64e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAA----ESRQKKLEMEK-------LQLQALEQEHKKLA-----ARLEEERGKNKQVVlMLVKECKQLSGKV 167
Cdd:pfam12128 620 QAAAEEQLVQAngelEKASREETFARtalknarLDLRRLFDEKQSEKdkknkALAERKDSANERLN-SLEAQLKQLDKKH 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 ---IEE--AQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEID 242
Cdd:pfam12128 699 qawLEEqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
170
....*....|.
gi 1390010537 243 KMRKMIEQLKR 253
Cdd:pfam12128 779 TLERKIERIAV 789
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
101-226 |
1.66e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK-KLAARLEEERGKNKQVVLMLVKECKQLSGK-------VIEEAQ 172
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeakakaeAEAERK 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1390010537 173 KLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAK 226
Cdd:TIGR02794 144 AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK 197
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
80-231 |
1.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 80 KEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLML- 156
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreEYLELSRELAGLRAELEELEKRREEIKKTLe 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1390010537 157 -VKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELsaeKRRSTEMEAQMEKQL-SEFdTEREQLRAKLNREE 231
Cdd:PRK03918 698 kLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL---KERALSKVGEIASEIfEEL-TEGKYSGVRVKAEE 770
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
119-250 |
1.69e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 41.18 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 119 KKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNE-----LEE 193
Cdd:pfam09756 1 KKLGAKKRAKLELKEAKRQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQeeyekLKS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 194 ELSAEKRRSTEMEAQMEKQLSE----FDTER-----EQLRAKLNreeahtTDLKEEIDKMRKMIEQ 250
Cdd:pfam09756 81 QFVVEEEGTDKLSAEDESQLLEdfinYIKLKkvvllEELAAEFG------LKTQDVIDRIQDLEEQ 140
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
5-256 |
1.78e-03 |
|
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: 43.11 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 5 LHPQKKKEFDvDTLSKSELRMllSVMEGELEARDLVIEALRARRKEVFIQERygrfNLNDPFLALQRDYEAGA------- 77
Cdd:TIGR00606 706 LAPDKLKSTE-SELKKKEKRR--DEMLGLAPGRQSIIDLKEKEIPELRNKLQ----KVNRDIQRLKNDIEEQEtllgtim 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 78 GDKEKKPVCTNPLSILEAVMAHCKKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHK--------KLAARLEEERGKN 149
Cdd:TIGR00606 779 PEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldtvvskiELNRKLIQDQQEQ 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 150 KQVVLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKqlseFDTEREQLRAKLNR 229
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK----DQQEKEELISSKET 934
|
250 260 270
....*....|....*....|....*....|....*
gi 1390010537 230 E----EAHTTDLKEEIDK----MRKMIEQLKRGSD 256
Cdd:TIGR00606 935 SnkkaQDKVNDIKEKVKNihgyMKDIENKIQDGKD 969
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
792-817 |
1.80e-03 |
|
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: 37.24 E-value: 1.80e-03
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
116-248 |
1.81e-03 |
|
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: 40.24 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 116 SRQKKLEMEKLQlQALEQEHKKLAARLEEERGKNkqvvLMLVKEckqlsgkvieeAQKLEDVMAKLEEEKKKTNELEEEL 195
Cdd:pfam12474 31 ERQQKQQIEKLE-QRQTQELRRLPKRIRAEQKKR----LKMFRE-----------SLKQEKKELKQEVEKLPKFQRKEAK 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 196 saeKRRSTEMEAQMEKQlsefdtEREQLRAKLnreEAHTTDLKEEIDKMRKMI 248
Cdd:pfam12474 95 ---RQRKEELELEQKHE------ELEFLQAQS---EALERELQQLQNEKRKEL 135
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
102-252 |
1.95e-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: 43.24 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 102 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAArlEEERGKnkqvvLMLVKECKQLSgkviEEAQKLEDvm 178
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 179 aKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTeREQLRAKLNRE-EAHTTDLKE---EIDKMRKMIEQLK 252
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEEkaaAYDKLEKTKNRLQ 579
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-254 |
2.00e-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: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 122 EMEKlQLQALEQE------HKKLAARLEEergknKQVVLMLVKeckqlsgkvieeaqkLEDVMAKLEEEKKKTNELEEEL 195
Cdd:COG1196 197 ELER-QLEPLERQaekaerYRELKEELKE-----LEAELLLLK---------------LRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 196 SAEkrrstemeaqmEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLKRG 254
Cdd:COG1196 256 EEL-----------EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
97-215 |
2.01e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 97 MAHCKKMQERMSAQ------LAA-AESRQKKLEMEKLQLQALEQEH---KKLA-----------ARLEEERGKNKQVVLM 155
Cdd:pfam13904 41 ARKLEGLKLERQPLeayenwLAAkQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKA 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 156 LVKECKQLSGKVIEEAQklEDVMAKLEE-EKKKTNEL----EEELSAEKRRstEMEAQMEKQLSE 215
Cdd:pfam13904 121 AESASKSLAKPERKVSQ--EEAKEVLQEwERKKLEQQqrkrEEEQREQLKK--EEEEQERKQLAE 181
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
166-246 |
2.06e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 39.51 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 166 KVIEEA-QKLEDVMAKLEEEKKKT-NELEEElSAEKRRSTEMEAQMEKQ--LSEFDTEREQLRAKLnREEAhttdlKEEI 241
Cdd:COG2811 8 KEIKEAeEEADEIIEEAKEEREERiAEAREE-AEEIIEQAEEEAEEEAQerLEEAREEAEAEAEEI-IEEG-----EKEA 80
|
....*
gi 1390010537 242 DKMRK 246
Cdd:COG2811 81 EALKK 85
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
99-257 |
2.13e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 99 HCKkmqERMSAQLAAAESRQ-KKLEMEKLQLQALEQEHKKLAARLEEErGKNKQVVLMLVKECKQLSgkviEEAQKLEDV 177
Cdd:pfam10174 596 NDK---DKKIAELESLTLRQmKEQNKKVANIKHGQQEMKKKGAQLLEE-ARRREDNLADNSQQLQLE----ELMGALEKT 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSE-FDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQ---LKR 253
Cdd:pfam10174 668 RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEKDANIALLELSSSKKKKTQEEvmaLKR 747
|
....
gi 1390010537 254 GSDS 257
Cdd:pfam10174 748 EKDR 751
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
101-150 |
2.14e-03 |
|
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.
Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 37.52 E-value: 2.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 101 KKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAARLEEERGKNK 150
Cdd:cd14686 4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
93-252 |
2.24e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQ 172
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLEDVMAKLEEEKKKTNELEEELSAEKrrsteMEAQMEKQLSEFDTER-----EQLRAKLNREEAhTTDLKEEIDKMRKM 247
Cdd:pfam04012 119 QLAALETKIQQLKAKKNLLKARLKAAK-----AQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAELASAVDL 192
|
....*
gi 1390010537 248 IEQLK 252
Cdd:pfam04012 193 DAKLE 197
|
|
| DUF4355 |
pfam14265 |
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ... |
177-252 |
2.62e-03 |
|
Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.
Pssm-ID: 405026 [Multi-domain] Cd Length: 119 Bit Score: 39.60 E-value: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390010537 177 VMAKLEEEKKKTNELEEELSAEKRRSTEMEAQmEKQlsefDTEREQLRAKLNREEAHTTdLKEEIDKMRKMIEQLK 252
Cdd:pfam14265 8 VAKALATKKNNLEKEIEDEIKEAKKLAKMNAE-EKA----KYELEKLQKELEEEKAELA-RKELKAEARKMLSEKG 77
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
95-252 |
2.68e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.18 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 95 AVMAHCKKMQERMSAQlAAAESRQKKLEMEKLQLqALEQEHKklaarleeergknkQVVLMLVKECKQLSGKVIEEAQKL 174
Cdd:pfam15665 56 QTLEESLEQHERMKRQ-ALTEFEQYKRRVEEREL-KAEAEHR--------------QRVVELSREVEEAKRAFEEKLESF 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 175 EDVMAKLEEEKKKTneLEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLraklnrEEAHttdlKEEIDKMRKMIEQLK 252
Cdd:pfam15665 120 EQLQAQFEQEKRKA--LEELRAKHRQEIQELLTTQRAQSASSLAEQEKL------EELH----KAELESLRKEVEDLR 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
172-252 |
2.73e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 172 QKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqmekQLSEFDTEREQLRAKL--NREEAHTtdLKEEIDKMRKMIE 249
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNE----ELKELAEKRDELNAQVkeLREEAQE--LREKRDELNEKVK 74
|
...
gi 1390010537 250 QLK 252
Cdd:COG1340 75 ELK 77
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
67-250 |
2.83e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 67 LALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCKKMQERmsAQLAAAESRQKKLEMEKLQlQALEQEHKKLAARLEEER 146
Cdd:cd22656 97 LELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDK--AAKVVDKLTDFENQTEKDQ-TALETLEKALKDLLTDEG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 147 GKNKQvvlmlvKECKQLSGKvIEEAQK--LEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAqMEKQLSEFDTEREQLR 224
Cdd:cd22656 174 GAIAR------KEIKDLQKE-LEKLNEeyAAKLKAKIDELKALIADDEAKLAAALRLIADLTA-ADTDLDNLLALIGPAI 245
|
170 180
....*....|....*....|....*.
gi 1390010537 225 AKLNREEAHTTDLKEEIDKMRKMIEQ 250
Cdd:cd22656 246 PALEKLQGAWQAIATDLDSLKDLLED 271
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
112-252 |
3.01e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 112 AAAESRQKKLEMEKL--------QLQALEQEHKKlaaRLEEERGKNKQVvlmlvkecKQLSGKVIEEAQKledvMAKLEE 183
Cdd:pfam05622 109 LAEEAQALKDEMDILressdkvkKLEATVETYKK---KLEDLGDLRRQV--------KLLEERNAEYMQR----TLQLEE 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 184 EKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDT---EREQLRAKLNREEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:pfam05622 174 ELKKANALRGQLETYKRQVQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERLIIERDTLRETNEELR 245
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
118-275 |
3.02e-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: 41.72 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 118 QKKLEMEKlQLQALEQEHKKLAARLeeergknkqvvLMLVKECKQLSGKVIE-EAQKLEDVMA------KLEEE--KKKT 188
Cdd:pfam15905 87 QERGEQDK-RLQALEEELEKVEAKL-----------NAAVREKTSLSASVASlEKQLLELTRVnellkaKFSEDgtQKKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 189 NELEEEL-SAEKRRSTEMEA------QMEKQLSEFDTEREQLRAKL--------------NREEAHTTDLKEEIDKMRKM 247
Cdd:pfam15905 155 SSLSMELmKLRNKLEAKMKEvmakqeGMEGKLQVTQKNLEHSKGKVaqleeklvstekekIEEKSETEKLLEYITELSCV 234
|
170 180
....*....|....*....|....*...
gi 1390010537 248 IEQLKRGSDSKPSLSLPRKTKDRRLVSI 275
Cdd:pfam15905 235 SEQVEKYKLDIAQLEELLKEKNDEIESL 262
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
101-256 |
3.24e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQ-ERMSAQLAAAESRQK--KLEMEKLQLQALEQEHKKLAARLEEERGKNKQVV---LMLVKECKQLSGKVIEEAQK- 173
Cdd:pfam05010 11 EKARnEIEEKELEINELKAKyeELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEhaeIQKVLEEKDQALADLNSVEKs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 174 LEDVMAKLE------------EE--KKKTNELEEELSAEKRRSTEMEAQMEKQL-----------SEFDTEREQLRAKLN 228
Cdd:pfam05010 91 FSDLFKRYEkqkevisgykknEEslKKCAQDYLARIKKEEQRYQALKAHAEEKLdqaneeiaqvrSKAKAETAALQASLR 170
|
170 180
....*....|....*....|....*...
gi 1390010537 229 REEAHTTDLKEEIDKMRKMIEQLKRGSD 256
Cdd:pfam05010 171 KEQMKVQSLERQLEQKTKENEELTKICD 198
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
115-218 |
3.27e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 40.09 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 115 ESRQK-KLEMEKLQLQ-----ALEQEHKKLAARLEEERGK-NKQVVLMLVKEC-KQLSGKVIEEAQKLEDVMAKLEEEKK 186
Cdd:smart01071 39 QARVErMEEIKNLKYElimndHLNKRIDKLLKGLREEELSpETPTYNEMLAELqDQLKKELEEANGDSEGLLEELKKHRD 118
|
90 100 110
....*....|....*....|....*....|..
gi 1390010537 187 KTNELEEELsaeKRRSTEMEAQMEKQLSEFDT 218
Cdd:smart01071 119 KLKKEQKEL---RKKLDELEKEEKKKIWSVDT 147
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
105-252 |
3.38e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.27 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 105 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKL-----AARLEEergkNKQVvlmlvkecKQLSGKVIEEAQKLEDvma 179
Cdd:pfam10368 4 EKIYDHLEEAVELEKPFEEQQEPLVELEKKEQELyeeiiELGMDE----FDEI--------KKLSDEALENVEEREE--- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 180 KLEEEKKKTNELEEELSaekrrstEMEAQMEK-QLSEFDTEREQLRAKLN-REEAH---TTDLKEEIDKMRKMIEQLK 252
Cdd:pfam10368 69 LLEKEKESIEEAKEEFK-------KIKEIIEEiEDEELKKEAEELIDAMEeRYEAYdelYDAYKKALELDKELYEMLK 139
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
156-252 |
3.67e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 156 LVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE----ELSA--EKRRSTEMEAQMEKQ-LSEFDTEREQLRAKLN 228
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdptELDRakEKLKKLLQEIMIKVKkLEELEEELQELESKIE 242
|
90 100
....*....|....*....|....
gi 1390010537 229 REEAHTTDLKEEIDKMRKMIEQLK 252
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQCR 266
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-250 |
3.83e-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: 41.93 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 110 QLAAAESRQKKLEMEKLQ----LQALEQEHKKLAARL------EEERGKNKQVVLM----------------LVKECKQL 163
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEkeskISDLEDELNKDDFELkkenleKEIDEKNKEIEELkqtqkslkkkqeekqeLIDQKEKE 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 164 SGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDK 243
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
....*..
gi 1390010537 244 MRKMIEQ 250
Cdd:TIGR04523 678 IIELMKD 684
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
740-845 |
3.86e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.74 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 740 DCVRLLLSAEAQVNAADKNGFTPLCAAAAQGHF---ECVELLISYDANINHAADGGQTPLYLACKNGNK---ECIKLLLE 813
Cdd:PHA02798 90 DIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
|
90 100 110
....*....|....*....|....*....|....*..
gi 1390010537 814 AGTN-RSVKTTDGWTPVHA----AVDTGNVDSLKLLM 845
Cdd:PHA02798 170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
133-258 |
3.87e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 133 QEHKKLAARLEEERGKN---KQVVLMLVKEcKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEE-ELSAEKRRSTEMEAQ 208
Cdd:cd16269 149 EDREKLVEKYRQVPRKGvkaEEVLQEFLQS-KEAEAEAILQADQALTEKEKEIEAERAKAEAAEqERKLLEEQQRELEQK 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 209 MEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI--DKMRKMIEQLKRGSDSK 258
Cdd:cd16269 228 LEDQERSYEEHLRQLKEKMEEERENLLKEQERAleSKLKEQEALLEEGFKEQ 279
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
317-570 |
3.88e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.14 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 317 PLVSANAKGSVCTSATMARP-GIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPlPSNAAPP----- 390
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAvPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAP-PAAPAPPatadr 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 391 -TAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAarfrfqgnANDPDQNGNTTQSPPSRDVSPTSRdnlVAKQL 469
Cdd:PRK07003 439 gDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSAS--------APASDAPPDAAFEPAPRAAAPSAA---TPAAV 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 470 ARNTVTQALSRFTSPQAGAPSRPGVPPTGdvgthPPVGRTSLKTHGVA-----------RV--DRG-NPPPIPPKKPGLS 535
Cdd:PRK07003 508 PDARAPAAASREDAPAAAAPPAPEARPPT-----PAAAAPAARAGGAAaaldvlrnagmRVssDRGaRAAAAAKPAAAPA 582
|
250 260 270
....*....|....*....|....*....|....*
gi 1390010537 536 QTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTP 570
Cdd:PRK07003 583 AAPKPAAPRVAVQVPTPRARAATGDAPPNGAARAE 617
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
368-665 |
4.23e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 368 PSTGSTPDPTSSTPPLPSNAAPPTAQTPGIAPQNSQAPPMhslhspcANTSLHPGLNPRIQAARFRFQGNAndpdqngnt 447
Cdd:PRK07003 360 PAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAV-------TAVTGAAGAALAPKAAAAAAATRA--------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 448 tQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGAPSRPGVPPTGDVGTHPPVGRTSlkthgvarvdrgnpppi 527
Cdd:PRK07003 424 -EAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAP----------------- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 528 ppkkpglsqTPSPPHPQLKVIIDSSRASNTGAKVDNKTVASTPSSLPQgnrvineenlPKSSSPQL-PPKPSIDLTVAPA 606
Cdd:PRK07003 486 ---------PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAA----------AAPPAPEArPPTPAAAAPAARA 546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390010537 607 GCAVSAL-------------------ATSQVGAWPAATPglnQPACSDSSLVIPTTIAFCSSINPVSASSCR-PGASDS 665
Cdd:PRK07003 547 GGAAAALdvlrnagmrvssdrgaraaAAAKPAAAPAAAP---KPAAPRVAVQVPTPRARAATGDAPPNGAARaEQAAES 622
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
8-258 |
4.36e-03 |
|
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: 41.96 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 8 QKKKEFDVDtlsKSELRMLLSVMEGELEARDLVIEALrARRKEVFIQERygrfnlnDPFLALQRDyeagagdkekkpvct 87
Cdd:TIGR00606 340 QEKTELLVE---QGRLQLQADRHQEHIRARDSLIQSL-ATRLELDGFER-------GPFSERQIK--------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 88 NPLSILEAVMAHCKKMQERMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGKnkqvvlmLVKECKQLSgKV 167
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADL------QSKERLKQEQADEIRDEKKGLGRTIELKKEI-------LEKKQEELK-FV 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQKLEDVMAKLEEEKKKTNELEEELS-AEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEA----HTTDLKEEID 242
Cdd:TIGR00606 460 IKELQQLEGSSDRILELDQELRKAERELSkAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEqlnhHTTTRTQMEM 539
|
250
....*....|....*.
gi 1390010537 243 KMRKMIEQLKRGSDSK 258
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIK 555
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
101-277 |
4.38e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.16 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEAQKLEDVMAK 180
Cdd:PRK06669 28 KVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 181 LEEEKKktnELEEELSAEKRRSTEMEAQmEKQLSEFDTEREQLRA---KLNRE-EAHTTDLKEEIDKMRKMI--EQLKRG 254
Cdd:PRK06669 108 WEEELE---RLIEEAKAEGYEEGYEKGR-EEGLEEVRELIEQLNKiieKLIKKrEEILESSEEEIVELALDIakKVIKEI 183
|
170 180
....*....|....*....|....*....
gi 1390010537 255 SDSKPSLSLP------RKTKDRRLVSISV 277
Cdd:PRK06669 184 SENSKEIALAlvkellKEVKDATDITIRV 212
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
101-262 |
4.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEER-----GKNKQVVLMLVKECKQL---SGKVIEEAQ 172
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElqreeERLVQKEEQLDARAEKLdnlENQLEEREK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 173 KLEDVMAKLEEEKKKT-NELEEelsAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMIEQL 251
Cdd:PRK12705 113 ALSARELELEELEKQLdNELYR---VAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRI 189
|
170
....*....|.
gi 1390010537 252 KRGSDSKPSLS 262
Cdd:PRK12705 190 ASETASDLSVS 200
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
112-277 |
4.63e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 112 AAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLSGKVIEEA--------------QKLEDV 177
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAkkeadeiikelrqlQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 178 MAK---LEEEKKKTNE----LEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLrAKLNREEAhttDLKEEIDKMRKMIEQ 250
Cdd:PRK00409 603 SVKaheLIEARKRLNKanekKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL-SIPDDKEA---IVQAGIMKMKVPLSD 678
|
170 180
....*....|....*....|....*..
gi 1390010537 251 LKRGSDSKPSLSLPRKTKDRRLVSISV 277
Cdd:PRK00409 679 LEKIQKPKKKKKKKPKTVKPKPRTVSL 705
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
309-496 |
4.77e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.51 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 309 PVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLIGASVPAFPPPSANKIEENGPSTGSTPDPTSSTPPLPSNAA 388
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 389 PPTAQTPGIAPQNSQAPPMHSLHSPCANTSLHPGLNPRIQAARfrfQGNANDPDQNGNTTQSPPsrdvsPTSRDNLVAKQ 468
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQ---AAQGASAPSPAADDPVPL-----PPEPDDPPDPA 752
|
170 180
....*....|....*....|....*...
gi 1390010537 469 LARNTVTQALSRFTSPQAGAPSRPGVPP 496
Cdd:PRK07764 753 GAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
726-826 |
4.87e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.80 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 726 GHSALYSAAKNGHTDCVRLLLSAEAQVNAADkNGFtPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNK 805
Cdd:PHA02791 30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107
|
90 100
....*....|....*....|.
gi 1390010537 806 ECIKLLLEAGTNRSVKTTDGW 826
Cdd:PHA02791 108 QTVKLFVKKNWRLMFYGKTGW 128
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
760-848 |
4.90e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 760 FTPLCAAAAQGHFECVELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTdgWTPVHAAVDTGNVD 839
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVE 115
|
....*....
gi 1390010537 840 SLKLLMYHR 848
Cdd:PHA02878 116 IFKIILTNR 124
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
307-406 |
5.54e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 41.08 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 307 TMPVKPSTGSPLVSANAKGSVCTSATMARPGIDRQASYGDLI-------GASVPAFPPPSANKIEENGPSTGSTPDPTSS 379
Cdd:PRK10905 122 TLPTEPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIepkkpqaTAKTEPKPVAQTPKRTEPAAPVASTKAPAAT 201
|
90 100
....*....|....*....|....*..
gi 1390010537 380 TPPLPSNAApPTAQTPGIAPQNSQAPP 406
Cdd:PRK10905 202 STPAPKETA-TTAPVQTASPAQTTATP 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-250 |
5.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 22 ELRMLLSVMEGELEARDLVIEALRARRkEVFIQERYGRFNLNDpFLALQRDYEA--------GAGDKEkkpvctnpLSIL 93
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID-VASAEREIAEleaelerlDASSDD--------LAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 94 EAVMAHCKKMQERMSAQLAAAESRQKKLEMeklQLQALEQEHKKLAARLEE-ERGKNKQVVLMLVKECKQLSGKVIEE-- 170
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERel 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 171 AQKLEDVMAKLEEEK-KKTNELEEELSAEKRR----STEMEAQMEkQLSEFDTEREQL-------------RAKLNREEA 232
Cdd:COG4913 768 RENLEERIDALRARLnRAEEELERAMRAFNREwpaeTADLDADLE-SLPEYLALLDRLeedglpeyeerfkELLNENSIE 846
|
250
....*....|....*...
gi 1390010537 233 HTTDLKEEIDKMRKMIEQ 250
Cdd:COG4913 847 FVADLLSKLRRAIREIKE 864
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
102-211 |
6.24e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 102 KMQ----ERMSAQLAA--AESRQKKLEMEKLQ-----------LQALEQEHKKLAARLEE-----ERGKNKQV------- 152
Cdd:pfam12718 1 KMNslklEAENAQERAeeLEEKVKELEQENLEkeqeikslthkNQQLEEEVEKLEEQLKEakekaEESEKLKTnnenltr 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 153 -VLMLVKECKQLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEK 211
Cdd:pfam12718 81 kIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
101-256 |
6.42e-03 |
|
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: 41.04 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAaesRQKKLEMEKLQLQALEQehKKLAARLEEERGKNKQVVLMlvkECKQLSGKVIEEAQKLEDVMAK 180
Cdd:pfam15964 307 KERDDLMSALVSV---RSSLAEAQQRESSAYEQ--VKQAVQMTEEANFEKTKALI---QCEQLKSELERQKERLEKELAS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 181 ------------LEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam15964 379 qqekraqekealRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQL 458
|
....*...
gi 1390010537 249 EQLKRGSD 256
Cdd:pfam15964 459 NQTKMKKD 466
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
169-251 |
6.49e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 39.80 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 169 EEAQKLEDVMAKLEEEKKKTNELEEELS---AEKRRSTEMEAQMEKQL----SEFDTER----EQLRAK---LNREEAHT 234
Cdd:pfam06785 80 LDAEGFKILEETLEELQSEEERLEEELSqkeEELRRLTEENQQLQIQLqqisQDFAEFRleseEQLAEKqllINEYQQTI 159
|
90
....*....|....*..
gi 1390010537 235 TDLKEEIDKMRKMIEQL 251
Cdd:pfam06785 160 EEQRSVLEKRQDQIENL 176
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
127-252 |
6.76e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 127 QLQALEQEHKKLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEE-------AQKLEDVMAKLEEEKKKTNELEEE-- 194
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLEseeKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEEFSQFVELTESgd 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 195 -------LSAEKRRSTEMEAQMEK---QLSEFDTE-REQLR------AKLNRE---------EAHTTDLKEEIDKMRKMI 248
Cdd:PRK04778 193 yveareiLDQLEEELAALEQIMEEipeLLKELQTElPDQLQelkagyRELVEEgyhldhldiEKEIQDLKEQIDENLALL 272
|
....
gi 1390010537 249 EQLK 252
Cdd:PRK04778 273 EELD 276
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
93-236 |
6.91e-03 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 38.73 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 93 LEAVMAHCKKMQERMSAQLAAAesrQKKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmlvkecKQLSGKVIEEAQ 172
Cdd:COG2882 7 LQTLLDLAEKEEDEAARELGQA---QQALEQAEEQLEQLEQYREEYEQRLQQ----------------KLQQGLSAAQLR 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 173 KLEDVMAKLEEE----KKKTNELEEELsaEKRRSTEMEAQMEKQLseFDT----EREQLRAKLNREEAHTTD 236
Cdd:COG2882 68 NYQQFIARLDEAieqqQQQVAQAEQQV--EQARQAWLEARQERKA--LEKlkerRREEERQEENRREQKELD 135
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
168-252 |
6.94e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.84 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 168 IEEAQKLEDVMAKLEEEK----KKTNELEEELSAekrrstemeAQMEKQLSEFDtEReQLRAKLNREEAHTTDLKEEIDK 243
Cdd:pfam11559 51 LEFRESLNETIRTLEAEIerlqSKIERLKTQLED---------LERELALLQAK-ER-QLEKKLKTLEQKLKNEKEELQR 119
|
....*....
gi 1390010537 244 MRKMIEQLK 252
Cdd:pfam11559 120 LKNALQQIK 128
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
167-272 |
6.96e-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: 41.03 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 167 VIEEAQKLEdvmAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMRK 246
Cdd:pfam07888 25 VVPRAELLQ---NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110
....*....|....*....|....*....|
gi 1390010537 247 MIEQLKRGSDS----KPSLSLPRKTKDRRL 272
Cdd:pfam07888 102 KYKELSASSEElseeKDALLAQRAAHEARI 131
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
81-253 |
7.25e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.32 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 81 EKKPVCTNPLSILEAvmAHCKKMQErMSAQLaaaesrQKKLEMEKLQLQALEQEHKKLAARLEEERGK------------ 148
Cdd:pfam15397 45 QQYEKFGTIISILEY--SNKKQLQQ-AKAEL------QEWEEKEESKLNKLEQQLEQLNAKIQKTQEElnflstykdkey 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 149 -NKQV-VLMLVKECKQLSGKVIEEAQKLED----VMAKLEEEK-KKTNELEEELSAEKRRSTEmEAQMEKQLSEFDTERE 221
Cdd:pfam15397 116 pVKAVqIANLVRQLQQLKDSQQDELDELEEmrrmVLESLSRKIqKKKEKILSSLAEKTLSPYQ-ESLLQKTRDNQVMLKE 194
|
170 180 190
....*....|....*....|....*....|..
gi 1390010537 222 QLRAKLNREEahttdLKEEIDKMRKMIEQLKR 253
Cdd:pfam15397 195 IEQFREFIDE-----LEEEIPKLKAEVQQLQA 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-251 |
7.35e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 170 EAQKLEDVMAKLEEE-----------KKKTNELEEELSAEKRRSTEMEAQ---MEKQLSEFDTEREQLRAKLNREEAHTT 235
Cdd:TIGR02168 678 EIEELEEKIEELEEKiaelekalaelRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKELT 757
|
90
....*....|....*.
gi 1390010537 236 DLKEEIDKMRKMIEQL 251
Cdd:TIGR02168 758 ELEAEIEELEERLEEA 773
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
775-848 |
7.38e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 41.14 E-value: 7.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 775 VELLISYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGTNRSVKTTDGWTPVHAAV-DTGNVDSLKLLMYHR 848
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
101-253 |
7.44e-03 |
|
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: 40.88 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 101 KKMQERMSAQLAAAESRQKKL----EMEKL--QLQALEQEHKKLAARLEEERGKNKQVVLMLVKECKQLsgkviEEAQKL 174
Cdd:pfam05557 359 RAILESYDKELTMSNYSPQLLerieEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-----RQQESL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 175 EDVMAKLEEE---KKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQ---LRAKLNREEAHTTDLKEEIDKMRKMI 248
Cdd:pfam05557 434 ADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKtkvLHLSMNPAAEAYQQRKNQLEKLQAEI 513
|
....*
gi 1390010537 249 EQLKR 253
Cdd:pfam05557 514 ERLKR 518
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
694-849 |
7.48e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.83 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 694 TLLQQAAAQGNVTLLSMLLnEEGLDINYSC-------EDGHSALY------SAAKN-GHTDCVRLLLSAEAQVNAADKNG 759
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLL-ERGASVPARAcgdffvkSQGVDSFYhgesplNAAAClGSPSIVALLSEDPADILTADSLG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 760 FTPLCAAAAQGHF---------ECVELLISYDANI----------NHAadgGQTPLYLACKNGNKECIKLLLEagTNRSV 820
Cdd:TIGR00870 209 NTLLHLLVMENEFkaeyeelscQMYNFALSLLDKLrdskelevilNHQ---GLTPLKLAAKEGRIVLFRLKLA--IKYKQ 283
|
170 180 190
....*....|....*....|....*....|....*....
gi 1390010537 821 KTTDGWT--PVH-AAVDTGNVDS-------LKLLMYHRI 849
Cdd:TIGR00870 284 KKFVAWPngQQLlSLYWLEELDGwrrkqsvLELIVVFVI 322
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
164-237 |
7.51e-03 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 38.15 E-value: 7.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390010537 164 SGKVIEEAQKLEDVMAKLEEE----KKKTNELEEELSAEKrrstEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDL 237
Cdd:pfam04871 3 KSELESEASSLKNENTELKAElqelSKQYNSLEQKESQAK----ELEAEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
114-258 |
7.52e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 114 AESRQKKLEMEKLQLQALEqehkkLAARLEEERG---KNKQVVLMLVKECKQLSGKVIEEAQKLEdvmAKLEEEKKKTNE 190
Cdd:pfam07888 272 AELHQARLQAAQLTLQLAD-----ASLALREGRArwaQERETLQQSAEADKDRIEKLSAELQRLE---ERLQEERMEREK 343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390010537 191 LEEELSAEKRRStemeaqmEKQLSEFDTEREQLRAKL----NREEAHTTDLKEEIDKMRKMIEQLKRGSDSK 258
Cdd:pfam07888 344 LEVELGREKDCN-------RVQLSESRRELQELKASLrvaqKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| Nnf1 |
pfam03980 |
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is ... |
150-241 |
8.44e-03 |
|
Nnf1; NNF1 is an essential yeast gene that is necessary for chromosome segregation. It is associated with the spindle poles and forms part of a kinetochore subcomplex called MIND.
Pssm-ID: 461118 Cd Length: 103 Bit Score: 37.61 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 150 KQVVLMLVKECKQLSGKVIEEaqklEDVMAKLeeekkktNELEE-ELSAEKRRSTEMEAQMEKQL-----------SEFD 217
Cdd:pfam03980 8 RQMVEFLQESCREEFEEILEE----RDVVAKL-------NELDElIEEAKERREEGEGPAWRPSVppeelirahlaPYKQ 76
|
90 100
....*....|....*....|....
gi 1390010537 218 TEREQLRAKLNREEAHTTDLKEEI 241
Cdd:pfam03980 77 KQLEQLNARLQKLEAENAALAEEV 100
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
9-311 |
8.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 9 KKKEFDVDTLsKSELRML---LSVMEGELEArdlVIEALRARRKEV-FIQERYGRFNLNdpflaLQRDYEAGAGDKEKkp 84
Cdd:COG4372 34 RKALFELDKL-QEELEQLreeLEQAREELEQ---LEEELEQARSELeQLEEELEELNEQ-----LQAAQAELAQAQEE-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 85 vctnplsiLEAVMAHCKKMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAARLEEERGKNKQVVLMLVKECK 161
Cdd:COG4372 103 --------LESLQEEAEELQeelEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 162 QLSGKVIEEAQKLEDVMAKLEEEKKKTNELEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEI 241
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1390010537 242 DKM---RKMIEQLKRGSDSKPSLSLPRKTKDRRLVSISVGTEGTVTRSVACQTDLVTENADHMKKLPLTMPVK 311
Cdd:COG4372 255 VILkeiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
122-276 |
8.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 122 EMEKLQLQALEQEHKKLAARLEEErGknkqvvLMLVKECKQLS-----GKVIEEAQKLEDVMAKLEEEKKKTNELEEELS 196
Cdd:PRK05771 5 RMKKVLIVTLKSYKDEVLEALHEL-G------VVHIEDLKEELsnerlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 197 AEKRRSTEmEAQmEKQLSEFDTEREQLRAKLNREeahtTDLKEEIDKMRKMIEQLK--RGSDSKPSLSLPRKTKDRRLVS 274
Cdd:PRK05771 78 KVSVKSLE-ELI-KDVEEELEKIEKEIKELEEEI----SELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT 151
|
..
gi 1390010537 275 IS 276
Cdd:PRK05771 152 VP 153
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
104-195 |
9.18e-03 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 38.10 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 104 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAR--LEEERGKNKQVVLMLVKecKQLSGKVIEEAQkLEDVMAKL 181
Cdd:pfam00836 44 LEEIQKKLEAAEERRKSLEAQKLKQLAEKREKEEEALQkaDEENNNFSKMAEEKLKQ--KMEAYKENREAQ-IAALKEKL 120
|
90
....*....|....
gi 1390010537 182 EEEKKKTNELEEEL 195
Cdd:pfam00836 121 KEKEKHVEEVRKNK 134
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
119-260 |
9.53e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 39.26 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 119 KKLEMEKLQLQALEQEHKKLAARLEEergknkqvvlmLVKECKQLsGKVIEE-AQKLEDvMAKLEEEKKKT-NELEEELS 196
Cdd:cd07596 4 QEFEEAKDYILKLEEQLKKLSKQAQR-----------LVKRRREL-GSALGEfGKALIK-LAKCEEEVGGElGEALSKLG 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1390010537 197 -AEKRRSTEMEAQMEKQLSEF-DTEREQLR----AKL---NREEA--HTTDLKEEIDKMRKMIEQLKRGSDSKPS 260
Cdd:cd07596 71 kAAEELSSLSEAQANQELVKLlEPLKEYLRycqaVKEtldDRADAllTLQSLKKDLASKKAQLEKLKAAPGIKPA 145
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
164-253 |
9.70e-03 |
|
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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390010537 164 SGKVIEEAQKLEDVMAKLEEEKKKtneLEEELsaekrrsTEMEAQMEKQLSEFDTEreqlRAKLNREEAhtTDLKEEIDK 243
Cdd:smart00935 6 VQKILQESPAGKAAQKQLEKEFKK---RQAEL-------EKLEKELQKLKEKLQKD----AATLSEAAR--EKKEKELQK 69
|
90
....*....|
gi 1390010537 244 MRKMIEQLKR 253
Cdd:smart00935 70 KVQEFQRKQQ 79
|
|
| |
