|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
36-179 |
1.15e-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: 174.71 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 36 LSKSELRMLLSVMEGELEARDLVIEALRARR-KEVFIQERYGRFNLNDPFLALQRDYEAGAG-----DKEKPVCTNPLSI 109
Cdd:pfam09727 2 LSKDDLLKLLSILEGELQARDIVIAVLKAEKvKQLLLEARYGFKYPSDPLLALQRDSELLRDqsqdeDVYEAMYEKPLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAAAESRQKK------------------------------------LEMEKLQLQALEQEHK 153
Cdd:pfam09727 82 LEKLVEKQRETQRRMLEQLAAAEKRHRRvireleeekrkhardtaqgddftyllekererlkqeLEQEKAQQKRLEKELK 161
|
170 180
....*....|....*....|....*.
gi 167555091 154 KLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:pfam09727 162 KLLEKLEEELSKQKQIALLLVKERKR 187
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
688-959 |
1.21e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 688 LLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNG 767
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 768 FTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 847
Cdd:COG0666 121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 848 SLKLLmyhrvpapgnslsaeepksglfsLNGGesppgsskpvvpADlINHADKEGWTAAHIAASKGFKNCLEILCRHGGL 927
Cdd:COG0666 201 IVKLL-----------------------LEAG------------AD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
|
250 260 270
....*....|....*....|....*....|..
gi 167555091 928 EPERRDKCNRTVHDVATDDCKHLLENLNALKI 959
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
702-943 |
5.62e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.16 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 781
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 782 CIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLmyhrvpapg 861
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL--------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 862 nslsaeepksglfsLNGGesppgsskpvvpADlINHADKEGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHD 941
Cdd:COG0666 173 --------------LEAG------------AD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALD 224
|
..
gi 167555091 942 VA 943
Cdd:COG0666 225 LA 226
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
702-837 |
4.89e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.18 E-value: 4.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFE 781
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 782 CIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPI 837
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
715-953 |
3.86e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.49 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 715 LLSMLLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN 794
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 795 HSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLmyhrvpapgnslsaeepksglf 874
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 875 sLNGGesppgsskpvvpADlINHADKEGWTAAHIAASKGFKNCLEILCRHGGlEPERRDKCNRTVHDVA-----TDDCKH 949
Cdd:COG0666 140 -LEAG------------AD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAaenghLEIVKL 204
|
....
gi 167555091 950 LLEN 953
Cdd:COG0666 205 LLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
738-825 |
7.74e-22 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 738 LYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYnANINHSaAGGQTPLYLACKTGNKECIK 817
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
|
....*...
gi 167555091 818 LLLEAGTD 825
Cdd:pfam12796 79 LLLEKGAD 86
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
704-794 |
1.38e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.78 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 704 LQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNaEARVDAADkNGFTPLCVAAAQGHFECI 783
Cdd:pfam12796 1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|.
gi 167555091 784 ELLTAYNANIN 794
Cdd:pfam12796 78 KLLLEKGADIN 88
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
771-855 |
2.05e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.70 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGtDRSIKTrDGWTPIHAAVDTGNVDSLK 850
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78
|
....*
gi 167555091 851 LLMYH 855
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
722-841 |
6.27e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 79.24 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 722 EEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQ 801
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 167555091 802 TPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 841
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
804-933 |
1.62e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.83 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 804 LYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHrvpapgnslsaeepksglfslnggespp 883
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167555091 884 gsskpvVPADLINHadkeGWTAAHIAASKGFKNCLEILCRHgGLEPERRD 933
Cdd:pfam12796 53 ------ADVNLKDN----GRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
703-852 |
9.05e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 72.75 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 703 LLQQAAAQGNVTLLSM-LLNEEGLDINYCCEDSHSALYSAAKNGHTDC---VRLLLNAEARVDAADKNGFTPL-CVAAAQ 777
Cdd:PHA03095 15 LYDYLLNASNVTVEEVrRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLhLYLYNA 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 778 GHFECIELLTAYNANINHSAAGGQTPL--YLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD--SLKLL 852
Cdd:PHA03095 95 TTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLL 173
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
707-853 |
1.79e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.59 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 707 AAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 787 TAYnANINHSAAGGQTpLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLM 853
Cdd:PLN03192 611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
711-856 |
1.93e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 71.23 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 711 GNVTLLSMLLNEeGLDINYCCEDSHSALYSAAKNGHTD--CVRLLLNAEARVDAADKngftplcvaaaqghfecIELLTA 788
Cdd:PHA03100 119 NSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLS 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 789 YNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
707-856 |
2.65e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.79 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 707 AAAQGNVTLLSMLLNEeGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:PHA02875 9 AILFGELDIARRLLDI-GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167555091 787 TAYNANINHSA-AGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA02875 88 LDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
134-476 |
9.37e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 70.53 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 134 RQKKLEME------KLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGK------VVEEAQKLEEVMVK---- 197
Cdd:pfam15921 684 RNKSEEMEtttnklKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEAMTNanke 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 198 ---LEEEKKKTSELEDQLSAEKQRSAG------------------MEAQLEKQLFEF--------DTEREQLRAKLTree 248
Cdd:pfam15921 764 khfLKEEKNKLSQELSTVATEKNKMAGelevlrsqerrlkekvanMEVALDKASLQFaecqdiiqRQEQESVRLKLQ--- 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 249 aHTTDLKEeidkmkkmmeqmKKGndgkPGLSLPRKTKDKRLASISVA---TEGPVTRSVAC-----QTDVVTESTDPVKK 320
Cdd:pfam15921 841 -HTLDVKE------------LQG----PGYTSNSSMKPRLLQPASFTrthSNVPSSQSTASflshhSRKTNALKEDPTRD 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 321 LP-----LSVPIKPSTGSPLVSTNTKGNVGPSALL---IRPGIDRQASHSDLGPSPPTALPSSASRIEE---NGPSAGNA 389
Cdd:pfam15921 904 LKqllqeLRSVINEEPTVQLSKAEDKGRAPSLGALddrVRDCIIESSLRSDICHSSSNSLQTEGSKSSEtcsREPVLLHA 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 390 PDLSNstPST----PSGTAPAAAQTLGAAPQNHSQAPPVHSLHSPCANTHPGLNPRIQAARfrfqgNANDPDqNGNNTQS 465
Cdd:pfam15921 984 GELED--PSScftfPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAK-----TIHSPD-SVKDSQS 1055
|
410
....*....|.
gi 167555091 466 PPSRDVSPTSR 476
Cdd:pfam15921 1056 LPIETTGKTCR 1066
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
702-943 |
3.52e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.30 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEeGLDINYCCEDSHSALYSAAKNGHTDCVRLL-----------------------LNAEA 758
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 759 RVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIH 838
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 839 AAVDTGNVDSLKLLMYHrvpapGNSLSAEepksglfsLNGGESPPGSS----KPVVPAdLINHA-----DKEGWTAAHIA 909
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH-----GNHIMNK--------CKNGFTPLHNAiihnRSAIEL-LINNAsindqDIDGSTPLHHA 261
|
250 260 270
....*....|....*....|....*....|....*
gi 167555091 910 ASKGF-KNCLEILCRHGGlEPERRDKCNRTVHDVA 943
Cdd:PHA02874 262 INPPCdIDIIDILLYHKA-DISIKDNKGENPIDTA 295
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
688-853 |
4.64e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.94 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 688 LLMSGGPAPLAGRPTL---LQQAAAQGNVTLLSMLL--NEEGLDINYccEDSHSALYSAAKNGHTDCVRLLLNAEARVDA 762
Cdd:PHA02875 53 LLMKHGAIPDVKYPDIeseLHDAVEEGDVKAVEELLdlGKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 763 ADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDG-WTPIHAAV 841
Cdd:PHA02875 131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
|
170
....*....|..
gi 167555091 842 DTGNVDSLKLLM 853
Cdd:PHA02875 211 ENNKIDIVRLFI 222
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
736-786 |
5.15e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.21 E-value: 5.15e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167555091 736 SALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
720-857 |
6.27e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 720 LNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGH-----FECIELLTAYNANIN 794
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 795 HSAAGGQTPLYLA--CKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDS--LKLLMYHRV 857
Cdd:PHA03100 101 APDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
712-855 |
1.06e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.06 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 712 NVTLLSMLL-----NEEGLDINYCCEDSHSALYSaaknghTDCVRLLLNAEARVDAADKN-GFTPLCVAAAQGHFECIEL 785
Cdd:PHA02878 113 NVEIFKIILtnrykNIQTIDLVYIDKKSKDDIIE------AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTEL 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167555091 786 LTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDT-GNVDSLKLLMYH 855
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
769-820 |
1.87e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.67 E-value: 1.87e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 167555091 769 TPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLL 820
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
272-703 |
1.99e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.12 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 272 NDGKPG-LSLPRKTKDK-RLASISVATEGPVTRSVACQTDVVTESTDPvkklplsvPIKPSTGSPLVSTNTKGNVGPSAl 349
Cdd:PHA03247 2654 DDPAPGrVSRPRRARRLgRAAQASSPPQRPRRRAARPTVGSLTSLADP--------PPPPPTPEPAPHALVSATPLPPG- 2724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 350 lirPGIDRQASHSdlGPSPPTALPSSASRIEENGPSAGNAPdlsnSTPSTPSGTAPAAAQTlgAAPQNHSQAPPVHSLhS 429
Cdd:PHA03247 2725 ---PAAARQASPA--LPAAPAPPAVPAGPATPGGPARPARP----PTTAGPPAPAPPAAPA--AGPPRRLTRPAVASL-S 2792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 430 PCANTHPglNPRIQAARfrfQGNANDPDQNGNNTQSPPSRDVSPTsrdnlvakqlarnTVTQALSRFTSPQAGASSRLGA 509
Cdd:PHA03247 2793 ESRESLP--SPWDPADP---PAAVLAPAAALPPAASPAGPLPPPT-------------SAQPTAPPPPPGPPPPSLPLGG 2854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 510 S--PGGDAGTCPPVGRTGLK--TPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQlrasnagakvdnkivasPPSTLPQGT 585
Cdd:PHA03247 2855 SvaPGGDVRRRPPSRSPAAKpaAPARPPVRRLARPAVSRSTESFALPPDQPERP-----------------PQPQAPPPP 2917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 586 KVVNEENVPKSSSPQLPPKPSIDLTVASAGCPvsALATSQVGAWPAETPGLNQPACTDsslVIPTTVAFRSSINPVSASS 665
Cdd:PHA03247 2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP--AGAGEPSGAVPQPWLGALVPGRVA---VPRFRVPQPAPSREAPASS 2992
|
410 420 430
....*....|....*....|....*....|....*...
gi 167555091 666 RSPgASDSLLVTASGWSPSLTpLLMSGGPAPLAGRPTL 703
Cdd:PHA03247 2993 TPP-LTGHSLSRVSSWASSLA-LHEETDPPPVSLKQTL 3028
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
39-249 |
1.81e-09 |
|
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: 59.94 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 39 SELRMLLsvmegELEARDLVIEALRARRKEvfIQERYGRfnLNDPFLALQRDYEAgagdkekpvctnplsiLEAVMAHCR 118
Cdd:COG1579 4 EDLRALL-----DLQELDSELDRLEHRLKE--LPAELAE--LEDELAALEARLEA----------------AKTELEDLE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 119 KMQERMSAQLAAAESRQKKLEmEKL-------QLQALEQE---HKKLAAHLEEErgknkhvvlmlvkeckqlsgkvveea 188
Cdd:COG1579 59 KEIKRLELEIEEVEARIKKYE-EQLgnvrnnkEYEALQKEiesLKRRISDLEDE-------------------------- 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167555091 189 qkLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKltREEA 249
Cdd:COG1579 112 --ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--REEL 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-258 |
3.09e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEvfiqerygrfnlndpflALQRDYEAGAGdkekp 101
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-----------------AQAEEYELLAE----- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 102 vctnpLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKL----QLQALEQEHKKLAA---HLEEERGKNKHVVLMLV 174
Cdd:COG1196 297 -----LARLEQDIARLEERRRELEERLEELEEELAELEEELEeleeELEELEEELEEAEEeleEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 175 KECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQ---LEKQLFEFDTEREQLRAKLTREEAHT 251
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEleeLEEALAELEEEEEEEEEALEEAAEEE 451
|
....*..
gi 167555091 252 TDLKEEI 258
Cdd:COG1196 452 AELEEEE 458
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
802-852 |
1.21e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167555091 802 TPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLL 852
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
118-259 |
2.18e-08 |
|
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: 58.01 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKLEMEK----------LQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQLSGKV 184
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERkeerkryrqeLEEQIEEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 185 VEEAQKLEEVMV------KLEEEKKKTSELEDQLSAEKQRS-AGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:pfam13868 123 EKQRQLREEIDEfneeqaEWKELEKEEEREEDERILEYLKEkAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE 202
|
..
gi 167555091 258 ID 259
Cdd:pfam13868 203 RD 204
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-257 |
2.83e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 114 MAHCRKMQERMSAQLAAAEsrqKKLEMEKLQLQALEQEHKKLAAHLEEERGK---NKHVVLMLVKECKQLSGKVVEEAQK 190
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 191 LEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAK-----LTREEAHTTDLKEE 257
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLE 827
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
771-869 |
3.06e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.37 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 850
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90 100
....*....|....*....|....*.
gi 167555091 851 LLMYHRVP-------APGNSLSAEEP 869
Cdd:PTZ00322 166 LLSRHSQChfelganAKPDSFTGKPP 191
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
702-764 |
5.76e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 5.76e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEEGLDinyCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAAD 764
Cdd:pfam12796 32 TALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
702-754 |
6.99e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 6.99e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167555091 702 TLLQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLL 754
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
711-853 |
9.64e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.51 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 711 GNVTLLSMLLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYN 790
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 791 AN-----------------------INHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVD 847
Cdd:PHA02874 92 VDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
....*.
gi 167555091 848 SLKLLM 853
Cdd:PHA02874 172 IIKLLL 177
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
111-253 |
1.04e-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: 57.11 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 111 EAVMAHCRKMQ---ERMSAQLAAAESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG--KNKHVVLMLVKECK------- 178
Cdd:pfam01576 906 ELLNDRLRKSTlqvEQLTTELAAERSTSQKSESAR---QQLERQNKELKAKLQEMEGtvKSKFKSSIAALEAKiaqleeq 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 179 --------QLSGKVVEEAQK-LEEVMVKLEEEKKKTSELEDQlsAEKqrSAGMEAQLEKQLFEfdTEREQLRA-----KL 244
Cdd:pfam01576 983 leqesrerQAANKLVRRTEKkLKEVLLQVEDERRHADQYKDQ--AEK--GNSRMKQLKRQLEE--AEEEASRAnaarrKL 1056
|
....*....
gi 167555091 245 TREEAHTTD 253
Cdd:pfam01576 1057 QRELDDATE 1065
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-258 |
1.14e-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: 56.99 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 24 AEAAKKEFDVdtlsKSELRMLlsvmEGELEARDLviEALRARRKEVFIQERygrfnlndpflALQRDYEAGAGDKEKpvC 103
Cdd:TIGR02168 209 AEKAERYKEL----KAELREL----ELALLVLRL--EELREELEELQEELK-----------EAEEELEELTAELQE--L 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 104 TNPLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQA----LEQEHKKLAAHLEEERGKNKHV---VLMLVKE 176
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanLERQLEELEAQLEELESKLDELaeeLAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 177 CKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLsaEKQRSAgmEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKE 256
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQL--ETLRSK--VAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
..
gi 167555091 257 EI 258
Cdd:TIGR02168 422 EI 423
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
40-259 |
1.18e-07 |
|
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: 55.70 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 40 ELRMLLSVMEgELEARDLVIEALRARRKEVFIQERygrfnlnDPFLALQRDYEAGAGDKEKpvctnplSILEAVMAHCRK 119
Cdd:pfam13868 99 EREQMDEIVE-RIQEEDQAEAEEKLEKQRQLREEI-------DEFNEEQAEWKELEKEEER-------EEDERILEYLKE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 120 MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNkhvvlmLVKECKQlsgkvvEEAQK-LEEVMVKL 198
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL------YQEEQER------KERQKeREEAEKKA 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 199 EEEKKKTSELEDQLsAEKQRSAGMEAQLEKQLFE-------FDTEREQLRAKLTRE--EAHTTDLKEEID 259
Cdd:pfam13868 232 RQRQELQQAREEQI-ELKERRLAEEAEREEEEFErmlrkqaEDEEIEQEEAEKRRMkrLEHRRELEKQIE 300
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
785-840 |
1.83e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 49.27 E-value: 1.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 785 LLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAA 840
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
276-702 |
1.95e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.49 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 276 PGLSLPRKTKDKRLASISVATEGPVTRSvacqtdvvteSTDPvkklplSVPIKPSTGSPLVSTN-TKGNVGPSALL--IR 352
Cdd:PHA03247 2475 PGAPVYRRPAEARFPFAAGAAPDPGGGG----------PPDP------DAPPAPSRLAPAILPDePVGEPVHPRMLtwIR 2538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 353 pGIDRQASHSDLGPSP---PTALPSSASRI--------EENGPSAG------NAPDLSNS--TPSTPSGTAPAAAQTLGA 413
Cdd:PHA03247 2539 -GLEELASDDAGDPPPplpPAAPPAAPDRSvppprpapRPSEPAVTsrarrpDAPPQSARprAPVDDRGDPRGPAPPSPL 2617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 414 APQNHSQAPPVHSlHSPCANTHPGLNPRIQAARFRFQGNANDPDQNGNNTQSPPSRDVSPTSRDNLVAKQLARNTVT--- 490
Cdd:PHA03247 2618 PPDTHAPDPPPPS-PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGslt 2696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 491 ----------------QALSRFTSPQAGASSRLGASPGGDAGTCPPVGRTGLKTPGAARvdrgnpppippkkpglsQTPS 554
Cdd:PHA03247 2697 sladpppppptpepapHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA-----------------RPAR 2759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 555 PPHPQLRASNAGAKVDnkiVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSidltvASAGCPVSALATSQVGAWPAETP 634
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAP---AAGPPRRLTRPAVASLSESRESLPSPWDPADPP-----AAVLAPAAALPPAASPAGPLPPP 2831
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 635 GLNQPAC-TDSSLVIPTTVAFRSSINPVSASSRSPGASDSLLVTASGWSPSLTPLlmsggPAPLAGRPT 702
Cdd:PHA03247 2832 TSAQPTApPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL-----ARPAVSRST 2895
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-259 |
2.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 122 ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHV-----VLMLVKECKQLSGKVVEEAQKLEEVMV 196
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 197 KLEEEKKKTSELEDQLSAEKQRSAGMEAQL-------EKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLeqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-259 |
2.77e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEAQ 189
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 190 KLEEVMVKLEEEKKKTSELEDQLSAEKQRsagmEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-258 |
3.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 21 GATAEAAKKEFDvdTLSKSELRMllsvmEGELEARDL--VIEALRARRKEVFIqerygRFNLNDPFLALQRDYEAGAGdk 98
Cdd:COG4913 224 FEAADALVEHFD--DLERAHEAL-----EDAREQIELlePIRELAERYAAARE-----RLAELEYLRAALRLWFAQRR-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 99 ekpvctnpLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEH--------KKLAAHLEEERGKNKHVV 170
Cdd:COG4913 290 --------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 171 LMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAH 250
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*...
gi 167555091 251 TTDLKEEI 258
Cdd:COG4913 442 LLALRDAL 449
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
702-855 |
3.24e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.89 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEeGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQ-GHF 780
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 781 ECIELLTAYNANIN-HSAAGGQTPLYLACKTGNKecIKLLLEAGTDRSIKTRDGWTPIHAAVDT-GNVDSLKLLMYH 855
Cdd:PHA02878 249 DILKLLLEHGVDVNaKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQyLCINIGRILISN 323
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
118-259 |
3.61e-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: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMS---AQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQL-------SGKVVEE 187
Cdd:pfam01576 99 KKMQQHIQdleEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-------LSKERKLLeerisefTSNLAEE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 188 AQKL----------EEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:pfam01576 172 EEKAkslsklknkhEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
..
gi 167555091 258 ID 259
Cdd:pfam01576 252 LE 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-259 |
4.32e-07 |
|
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: 55.07 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 30 EFDVDtlsKSELRMLLSVMEGELEARDLVIEALRAR----RKEVFIQERYgrfnlnDPFLALQRDYEAGAgdkekpvctn 105
Cdd:TIGR02169 167 EFDRK---KEKALEELEEVEENIERLDLIIDEKRQQlerlRREREKAERY------QALLKEKREYEGYE---------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 106 plsILEAVMAHcRKMQERMSAQLAAAESRQKKLEMEKLQL--------QALEQEHKKLAAHLEEERGKNKHVVLMLVKEC 177
Cdd:TIGR02169 228 ---LLKEKEAL-ERQKEAIERQLASLEEELEKLTEEISELekrleeieQLLEELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 178 KQLSGKVVE---EAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKL---------T 245
Cdd:TIGR02169 304 ASLERSIAEkerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevdkefaeT 383
|
250
....*....|....
gi 167555091 246 REEahTTDLKEEID 259
Cdd:TIGR02169 384 RDE--LKDYREKLE 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
109-257 |
4.90e-07 |
|
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: 54.52 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 109 ILEAVMAHCRKMQ-ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE-----ERGKNKHVVLML-VKECKQLS 181
Cdd:pfam07888 31 LLQNRLEECLQERaELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkeelRQSREKHEELEEkYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 182 GKVVEEAQKLeevMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEK----------QLFEFDTEREQLRAKLTREEAHT 251
Cdd:pfam07888 111 EELSEEKDAL---LAQRAAHEARIRELEEDIKTLTQRVLERETELERmkerakkagaQRKEEEAERKQLQAKLQQTEEEL 187
|
....*.
gi 167555091 252 TDLKEE 257
Cdd:pfam07888 188 RSLSKE 193
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
120-249 |
5.07e-07 |
|
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: 53.77 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 120 MQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLaahleEERGKNKHVVLMLVKECKQLSGKVVE---EAQKLEEVM 195
Cdd:pfam13868 82 IEEREQKrQEEYEEKLQEREQMDEIVERIQEEDQAEA-----EEKLEKQRQLREEIDEFNEEQAEWKElekEEEREEDER 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 196 V------KLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDtEREQLRAKLTREEA 249
Cdd:pfam13868 157 IleylkeKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA-ERDELRAKLYQEEQ 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-259 |
5.90e-07 |
|
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: 54.69 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 38 KSELRML---LSVMEGELEArdlVIEALRARRKEVFiQERYGRFNLNDPFLALQRDYEAGAGDKEKPVctnplSILEAVM 114
Cdd:TIGR02169 673 PAELQRLrerLEGLKRELSS---LQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLK-----ERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 115 AHCRKMQErmsaQLAAAESRQKKLEMEK----LQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKE-CKQLSGKVVEEAQ 189
Cdd:TIGR02169 744 EDLSSLEQ----EIENVKSELKELEARIeeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEeVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167555091 190 KLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLE---KQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlnGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
107-259 |
6.86e-07 |
|
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: 53.61 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 107 LSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQA-LEQEHKKLAAHLEE--ERGKNKHVVLML---------- 173
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELAELLRAlyRLGRQPPLALLLspedfldavr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 174 --------VKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLT 245
Cdd:COG4942 137 rlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
170
....*....|....
gi 167555091 246 REEAHTTDLKEEID 259
Cdd:COG4942 217 ELQQEAEELEALIA 230
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
296-701 |
7.00e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.41 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 296 TEGPVTRSVACQTDVVTESTDPVKKLPLSVPIKPSTGSPLVSTNTKGnvgpsallirPGIDRQASHSDLGPSPPTALPSS 375
Cdd:PHA03307 68 PTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSP----------DPPPPTPPPASPPPSPAPDLSEM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 376 ASRIEENGP-SAGNAPDLSNSTPSTPSGTA-PAAAQTLGAAPQNHSQAPPvhslhspcantHPGLNPRIQAARFRFQGNA 453
Cdd:PHA03307 138 LRPVGSPGPpPAASPPAAGASPAAVASDAAsSRQAALPLSSPEETARAPS-----------SPPAEPPPSTPPAAASPRP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 454 NDPDqngnntqsPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGASPGGDAGTCPPVGRTGLKTPGAAR 533
Cdd:PHA03307 207 PRRS--------SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 534 VDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVDNKIVASPPSTLPQGTK---VVNEENVPKSSSPQLPPKPSIDLT 610
Cdd:PHA03307 279 SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSsseSSRGAAVSPGPSPSRSPSPSRPPP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 611 VASAGCPVSALATSQVGAWPAETPGLNQPACTDSSLVIPTTVAFRSSINPVSASSRSPGASDSllvtASGWSPSLTPLLM 690
Cdd:PHA03307 359 PADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGA----ASGAFYARYPLLT 434
|
410
....*....|..
gi 167555091 691 -SGGPAPLAGRP 701
Cdd:PHA03307 435 pSGEPWPGSPPP 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-258 |
8.79e-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: 53.91 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 22 ATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFNLNDPFLALQRDYEAGAGDKEKP 101
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL--EERIAQLSKELTELEAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 102 vctnPLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKHVVLMLVKECKQLS 181
Cdd:TIGR02168 776 ----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-------TLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 182 GKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRA---KLTREEAHTTDLKEEI 258
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElesKRSELRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-259 |
9.73e-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: 53.91 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 9 EPDLSRAPGDAEGATAEAAKKEFDVDTLSK--SELRMLLSVMEGELEARDLVIEALRARRKEVfiQERYGRFN-----LN 81
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKelTELEAEIEELEERLEEAEEELAEAEAEIEEL--EAQIEQLKeelkaLR 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 82 DPFLALQRDYEA---GAGDKekpvcTNPLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQE-HKKLAA 157
Cdd:TIGR02168 803 EALDELRAELTLlneEAANL-----RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEElESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 158 HLEEERGKNKHVVLM------LVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELE-------DQLSAEKQRSAGMEA 224
Cdd:TIGR02168 878 LLNERASLEEALALLrseleeLSEELRELESKRSELRRELEELREKLAQLELRLEGLEvridnlqERLSEEYSLTLEEAE 957
|
250 260 270
....*....|....*....|....*....|....*
gi 167555091 225 QLEkqlFEFDTEREQLRAKLTReeahttdLKEEID 259
Cdd:TIGR02168 958 ALE---NKIEDDEEEARRRLKR-------LENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-259 |
1.06e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 107 LSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVE 186
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 187 EAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLE---KQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEelaEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
733-840 |
1.34e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 52.29 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 733 DSHSALYSAAKNGHTDCVRLLL----NAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANIN-HSAAGGQTPLYLA 807
Cdd:PHA02884 32 CIANILYSSIKFHYTDIIDAILklgaDPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYIS 111
|
90 100 110
....*....|....*....|....*....|...
gi 167555091 808 CKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAA 840
Cdd:PHA02884 112 VLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
110-258 |
1.95e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSgkvvEEAQ 189
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ----AQEELESLQ----EEAE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 190 KLEEVMVKLEEEKKKTSELEDQLSAEKQrsagmeaQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIA-------ELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
777-865 |
2.30e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 52.37 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 777 QGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMYHR 856
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
|
....*....
gi 167555091 857 VPAPGNSLS 865
Cdd:PHA02876 235 SNINKNDLS 243
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
135-258 |
3.10e-06 |
|
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: 47.99 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 135 QKKLEMEKlQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSgkvvEEAQKLEEVMVKLEEEKKKtseledqLSA 214
Cdd:pfam20492 6 REKQELEE-RLKQYEEETKKAQEELEESEET----AEELEEERRQAE----EEAERLEQKRQEAEEEKER-------LEE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 167555091 215 EKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:pfam20492 70 SAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEEL 113
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
712-860 |
3.32e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.56 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 712 NVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTD--CVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIEL--LT 787
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLL 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167555091 788 AYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLKLLMyHRVPAP 860
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL-AKNPSA 316
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
118-229 |
3.60e-06 |
|
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: 48.51 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAEsRQKKLEMEKLQLQALEQEHKKLaahlEEERgknkhvvlmlvKECKQLSGKVVEEAQKLEEVMVK 197
Cdd:pfam15346 37 AEVERRVEEARKIME-KQVLEELEREREAELEEERRKE----EEER-----------KKREELERILEENNRKIEEAQRK 100
|
90 100 110
....*....|....*....|....*....|..
gi 167555091 198 LEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQ 229
Cdd:pfam15346 101 EAEERLAMLEEQRRMKEERQRREKEEEEREKR 132
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
25-257 |
3.89e-06 |
|
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: 51.90 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 25 EAAKKEFDVDTLSKSELRMLLsvMEGELEARDLVIEALRARRKEvfiQERYGRFNLNDPFLALQRDYEAGAGDKEKpvct 104
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDL--EELKLQELKLKEQAKKALEYY---QLKEKLELEEEYLLYLDYLKLNEERIDLL---- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 105 npLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgkv 184
Cdd:pfam02463 243 --QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL---- 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167555091 185 veeaQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQlfEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:pfam02463 317 ----KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE--EEELEKLQEKLEQLEEELLAKKKLES 383
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
288-712 |
4.12e-06 |
|
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: 51.84 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 288 RLASISVATEGPVTRSVACqTDVVTESTDPVKKLPLSVPIKPSTGSPlvSTNTKGNVGPSALLIRPgidrQASHSdlgps 367
Cdd:pfam05109 387 RTFDITVSGLGTAPKTLII-TRTATNATTTTHKVIFSKAPESTTTSP--TLNTTGFAAPNTTTGLP----SSTHV----- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 368 pPTALPSSASrieeNGPSAGNApDLSNSTPS-TPSGTAPAaaqTLGAAPQNH---SQAPPVHSLHSPCANTHPglnpriq 443
Cdd:pfam05109 455 -PTNLTAPAS----TGPTVSTA-DVTSPTPAgTTSGASPV---TPSPSPRDNgteSKAPDMTSPTSAVTTPTP------- 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 444 aarfrfqgnandpdqngnNTQSPPSRDVSPTSrdNLVAKQLARNTVTQALSRFTsPQAGASSRLGASPGGDAgTCPPVGR 523
Cdd:pfam05109 519 ------------------NATSPTPAVTTPTP--NATSPTLGKTSPTSAVTTPT-PNATSPTPAVTTPTPNA-TIPTLGK 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 524 TglkTPGAARVdrgnpppippkkpglSQTPSPPHPQLRASNAGAKVDNKIVASPPSTlpqgtkvvneenvPKSSSpqlPP 603
Cdd:pfam05109 577 T---SPTSAVT---------------TPTPNATSPTVGETSPQANTTNHTLGGTSST-------------PVVTS---PP 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 604 KPSidltvasagcpVSALATSQVGAWPAETPGLNQPACTDSSLVIPTTVAFRSSINPVSASSRSPGASDSLLVTASGWSp 683
Cdd:pfam05109 623 KNA-----------TSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPASTS- 690
|
410 420
....*....|....*....|....*....
gi 167555091 684 slTPLLMSGGPAPlagRPTLLQQAAAQGN 712
Cdd:pfam05109 691 --THHVSTSSPAP---RPGTTSQASGPGN 714
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
118-248 |
4.80e-06 |
|
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: 47.22 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMsaqlaaaesRQKKLEMEKLQLQALEQEHKklAAHLEEERGKNKHvvlmlvkECKQLSgkvvEEAQKLEEVMVK 197
Cdd:pfam20492 9 QELEERL---------KQYEEETKKAQEELEESEET--AEELEEERRQAEE-------EAERLE----QKRQEAEEEKER 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 167555091 198 LEEEKKKTSELEDQLsAEKQRSAGMEAQL---EKQLFEFDTEREQLRAKLTREE 248
Cdd:pfam20492 67 LEESAEMEAEEKEQL-EAELAEAQEEIARleeEVERKEEEARRLQEELEEAREE 119
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
702-838 |
6.40e-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: 50.78 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEEGLDInyCCEDSH--SALYSAAKNGHTDCVRLLLNAEAR-----VDAADKNGFTPLCVA 774
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDL--FQRGALgeTALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 775 AAQGHFECIELLTAYNAN-INHSAAG-------------GQTPLYLACKTGNKECIKLLLEAGTDrsIKTRDGW--TPIH 838
Cdd:cd22192 97 VVNQNLNLVRELIARGADvVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLgnTVLH 174
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
134-249 |
6.94e-06 |
|
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: 47.73 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 134 RQKKLEMEKLQLQALEQEhkklaahlEEERgknkhvvlmLVKEckQLSGKVVEEAQKLEEVMVKLEEEKKKTSElEDQLS 213
Cdd:pfam05672 21 RQAREQREREEQERLEKE--------EEER---------LRKE--ELRRRAEEERARREEEARRLEEERRREEE-ERQRK 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 167555091 214 AEKQRSAGMEAQLEKQLfEFDTEREQLRAKLtREEA 249
Cdd:pfam05672 81 AEEEAEEREQREQEEQE-RLQKQKEEAEAKA-REEA 114
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
116-259 |
8.72e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 116 HCRKMQERMSAQLAAAESRQKKL--EMEKLQLQALEQEHK---KL------AAHLEEERGKNKHVVLMLVKECKQLSGKV 184
Cdd:pfam05483 524 NCKKQEERMLKQIENLEEKEMNLrdELESVREEFIQKGDEvkcKLdkseenARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 185 VEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLE--KQLFE--FDTEREQLRAKLTREEahttDLKEEID 259
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAsaKQKFEeiIDNYQKEIEDKKISEE----KLLEEVE 678
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-257 |
1.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSA-QLAAAESRQKKLEMEKLQLQALEQEHKKLAA-------HLEEERGKNKHVVLMLVKECKQLSGKVVEEAQ 189
Cdd:PTZ00121 1540 KKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 190 KLEEVMVKLEEEKKKTSELEDQLSAEKQRSagmeAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKA----EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
|
| PRK11331 |
PRK11331 |
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional |
1077-1357 |
1.18e-05 |
|
5-methylcytosine-specific restriction enzyme subunit McrB; Provisional
Pssm-ID: 183088 [Multi-domain] Cd Length: 459 Bit Score: 49.70 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 1077 LSGPQEGCLSSVTYTSMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIANQLALCMKHRQMaagfPCEIVRAEVDSGFS 1156
Cdd:PRK11331 162 MSKTESYCLEDALNDLFIPETTIETILKRLTIKKNIILQGPPGVGKTFVARRLAYLLTGEKA----PQRVNMVQFHQSYS 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 1157 KEQLV-------------DVFISNACLiPVKQFPvKKKIIVILENLEKSSLSELLGDFLAPLEN----RSTESPCTFQKG 1219
Cdd:PRK11331 238 YEDFIqgyrpngvgfrrkDGIFYNFCQ-QAKEQP-EKKYVFIIDEINRANLSKVFGEVMMLMEHdkrgENWSVPLTYSEN 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 1220 NgtSECYYFHENCFLLGTL--AKACLQGSDLLVQQHFRWVQLRWDCEPSQglLQRFLRRKAVSkfrgqlPAPCDPVCKIV 1297
Cdd:PRK11331 316 D--EERFYVPENVYIIGLMntADRSLAVVDYALRRRFSFIDIEPGFDTPQ--FRNFLLNKKAE------PSFVESLCQKM 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 1298 DwvisvwrQLNSCLARLGTpeaLLGPKY-----FLSCPVVPGHAQATvKWMSKLWNAIIAPRVQE 1357
Cdd:PRK11331 386 N-------ELNQEISKEAT---ILGKGFrighsYFCCGLEDGTSPDT-QWLKEIVMTDIAPLLEE 439
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
38-259 |
1.30e-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: 50.17 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 38 KSELRMLLSVMEGELEARDLVIEALRARRKEvfIQErygrfNLNDpfLALQRDYEAGAGDK---EKPVCTNPLSILEA-- 112
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKK--MQQ-----HIQD--LEEQLDEEEAARQKlqlEKVTTEAKIKKLEEdi 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 113 -VMAHC-------RK-MQER---MSAQLAAAESRQKklemeklQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQL 180
Cdd:pfam01576 141 lLLEDQnsklskeRKlLEERiseFTSNLAEEEEKAK-------SLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 181 SGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSA-----EKQRSAGMEAQ-----LEKQLFEFDTEREQLRAKLTREEAH 250
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQAalarlEEETAQKNNALkkireLEAQISELQEDLESERAARNKAEKQ 293
|
....*....
gi 167555091 251 TTDLKEEID 259
Cdd:pfam01576 294 RRDLGEELE 302
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-259 |
1.59e-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: 50.06 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAAAES-RQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvVLMLVKECKQLSGKVVEEA 188
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEELREELEELQEE----LKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 189 QKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGME----------AQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkqilrerlANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
.
gi 167555091 259 D 259
Cdd:TIGR02168 347 E 347
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
299-625 |
1.86e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 49.53 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 299 PVTRSVACQtDVVTESTDPVKKLPLSVPIKPS-----------TGSPLVSTNTKGNVGPSALLIRPgidrqaSHSDLGPS 367
Cdd:pfam05109 487 PVTPSPSPR-DNGTESKAPDMTSPTSAVTTPTpnatsptpavtTPTPNATSPTLGKTSPTSAVTTP------TPNATSPT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 368 PPTALPSSASRIeengPSAGNAPDLSNSTPSTPSGTAPAAAQTlgaAPQNHSQAPPVHSLHSPCANTHPGLNpriqAARF 447
Cdd:pfam05109 560 PAVTTPTPNATI----PTLGKTSPTSAVTTPTPNATSPTVGET---SPQANTTNHTLGGTSSTPVVTSPPKN----ATSA 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 448 RFQGNANDPDQNGNNTQSPPS---RDVSPTSRDNLV--------AKQLARNTVTQALSRFTSPQAGASSRLGASPGGDAG 516
Cdd:pfam05109 629 VTTGQHNITSSSTSSMSLRPSsisETLSPSTSDNSTshmplltsAHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 517 TCPPVGRTGLKTPGAARVDRGNPPPIppkkpglSQTPSPPHPQLRA----SNAGAKVDNKI-----------VASPP--- 578
Cdd:pfam05109 709 ASGPGNSSTSTKPGEVNVTKGTPPKN-------ATSPQAPSGQKTAvptvTSTGGKANSTTggkhttghgarTSTEPttd 781
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 167555091 579 ----STLPQgTKVVNEENVPKSSSPQLPPK---PSIDLTVASAGCPVSalATSQ 625
Cdd:pfam05109 782 yggdSTTPR-TRYNATTYLPPSTSSKLRPRwtfTSPPVTTAQATVPVP--PTSQ 832
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
146-259 |
2.25e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 146 QALE-QEHKKLAAHLEEERGKNKHVVLML---VKECKQLSGKV---VEEAQKLEEvmvKLEEEKKKTSELEDQLSaEKQR 218
Cdd:COG2433 380 EALEeLIEKELPEEEPEAEREKEHEERELteeEEEIRRLEEQVerlEAEVEELEA---ELEEKDERIERLERELS-EARS 455
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 167555091 219 SAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
752-807 |
2.26e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 2.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 752 LLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLA 807
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
130-259 |
2.32e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 130 AAESRQKKLemekLQLQALEQEhkklAAHLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELE 209
Cdd:COG1579 1 AMPEDLRAL----LDLQELDSE----LDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 210 DQLSAEKQRSAGMEAQL--------------------------EKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG1579 66 LEIEEVEARIKKYEEQLgnvrnnkeyealqkeieslkrrisdlEDEILELMERIEELEEELAELEAELAELEAELE 141
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
121-259 |
2.44e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 121 QERMSAQLaaaESRQKKLEMEKlqlQALEQEHKKLAAHLEEERG-----KNKHVVLMLV------------KECKQLSGK 183
Cdd:TIGR04523 403 QEKLNQQK---DEQIKKLQQEK---ELLEKEIERLKETIIKNNSeikdlTNQDSVKELIiknldntresleTQLKVLSRS 476
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 184 VVEEAQKLEEvmvKLEEEKKKTSELeDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:TIGR04523 477 INKIKQNLEQ---KQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
25-258 |
2.50e-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: 49.33 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 25 EAAK-KEFDVDTlsKSELRMllsvMEGELEARDLVIEALRARRKEV-FIQERYGrfnlndpfLALQRDYEAGAG-DKEKP 101
Cdd:pfam05483 86 EAEKiKKWKVSI--EAELKQ----KENKLQENRKIIEAQRKAIQELqFENEKVS--------LKLEEEIQENKDlIKENN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 102 VCTNPLSILEAVMAhcRKMQERMSAQLAAAESRQKKLEM-----------EKLQLQA----------LEQEHKKLAaHLE 160
Cdd:pfam05483 152 ATRHLCNLLKETCA--RSAEKTKKYEYEREETRQVYMDLnnniekmilafEELRVQAenarlemhfkLKEDHEKIQ-HLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 161 EE-----RGKNKHVVLMLVKeckqlsgkVVEEAQKLEEVMVKLEEEKKKTSELEDQlsaEKQRSAGMEAQLEKQlFEFDT 235
Cdd:pfam05483 229 EEykkeiNDKEKQVSLLLIQ--------ITEKENKMKDLTFLLEESRDKANQLEEK---TKLQDENLKELIEKK-DHLTK 296
|
250 260
....*....|....*....|...
gi 167555091 236 EREQLRAKLTREEAHTTDLKEEI 258
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDL 319
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
704-803 |
2.64e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 704 LQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECI 783
Cdd:PTZ00322 86 LCQLAASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
90 100
....*....|....*....|
gi 167555091 784 ELLTAYnaNINHSAAGGQTP 803
Cdd:PTZ00322 165 QLLSRH--SQCHFELGANAK 182
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
110-248 |
2.65e-05 |
|
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: 48.38 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAA--AESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKH-VVLMLVKECKQLsgkvVE 186
Cdd:pfam13868 171 REAEREEIEEEKEREIARLRAqqEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKArQRQELQQAREEQ----IE 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 187 EAQKLEEVMVKLEEE-----KKKTSELE--DQLSAEKQR------SAGMEAQLEkqlfefdtEREQLRAKLTREE 248
Cdd:pfam13868 247 LKERRLAEEAEREEEefermLRKQAEDEeiEQEEAEKRRmkrlehRRELEKQIE--------EREEQRAAEREEE 313
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-259 |
3.22e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 25 EAAKKEFDvDTLSK-SELRMLLSVMEGELEArdlvieaLRARRKEVfiQERYGRFNlndpflALQRDYEAGAGDKEKpvc 103
Cdd:PRK03918 196 KEKEKELE-EVLREiNEISSELPELREELEK-------LEKEVKEL--EELKEEIE------ELEKELESLEGSKRK--- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 104 tnplsiLEAVMAHCRKMQERMSAQLAAAESRQKKLEmeklQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKQLSGK 183
Cdd:PRK03918 257 ------LEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYEEYLDE--------LREIEKRLSR 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 184 VVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGME--AQLEKQLFEFDTEREQLRAKLTREEAHttDLKEEID 259
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLTGLTPE--KLEKELE 394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
48-259 |
3.30e-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: 49.02 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 48 MEGELEARDLVIEALRARRKEVFIQERYGRFNLNDpflaLQRDYE----------AGAGDKEKPvctnpLSILEAVMAHc 117
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD----LQRELEearasrdeilAQSKESEKK-----LKNLEAELLQ- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 rkMQErmsaQLAAAESRQKKLEMEKLQLQ-----------ALEQEHKKLAA---HLEEERGKNKHVVLML-------VKE 176
Cdd:pfam01576 845 --LQE----DLAASERARRQAQQERDELAdeiasgasgksALQDEKRRLEAriaQLEEELEEEQSNTELLndrlrksTLQ 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 177 CKQLSGKVVEE---AQKLEEVMVKLE----EEKKKTSELEDQLSAeKQRS--AGMEA---QLEKQLfEFDTEREQLRAKL 244
Cdd:pfam01576 919 VEQLTTELAAErstSQKSESARQQLErqnkELKAKLQEMEGTVKS-KFKSsiAALEAkiaQLEEQL-EQESRERQAANKL 996
|
250 260 270
....*....|....*....|....*....|
gi 167555091 245 TR---------------EEAHTTDLKEEID 259
Cdd:pfam01576 997 VRrtekklkevllqvedERRHADQYKDQAE 1026
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
702-841 |
3.35e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.52 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 702 TLLQQAAAQGNVTLLSMLLNEEGLDINYCCEDSHSALYSAAKNGH-TDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHF 780
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 781 ECIEL-LTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV 841
Cdd:PHA02876 355 KDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-290 |
3.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 130 AAESRQKKLEMEKLQLQALEQehKKLAAHLEEERGKNKhvvlmlVKECKqlsgKVVEEAQKLEEVMVKLEEEKKKTSELE 209
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEE--KAEAAEKKKEEAKKK------ADAAK----KKAEEKKKADEAKKKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 210 DQlSAEKQRSAGMEAQLEKQlfefdteREQLRAKLTREEAHTTD-LKEEIDKMKKMMEQMKKGNDGKPGLSLPRKTKDKR 288
Cdd:PTZ00121 1412 KA-AAAKKKADEAKKKAEEK-------KKADEAKKKAEEAKKADeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
..
gi 167555091 289 LA 290
Cdd:PTZ00121 1484 KA 1485
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
366-726 |
3.44e-05 |
|
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: 48.61 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 366 PSPPTALPSSASRIEENGPSAGNAPdlsnSTPSTPSGTAPAAAQtlgaAPQNHSQAPPVHSLHSPCANTHPglnPRIQAA 445
Cdd:pfam03154 177 QSGAASPPSPPPPGTTQAATAGPTP----SAPSVPPQGSPATSQ----PPNQTQSTAAPHTLIQQTPTLHP---QRLPSP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 446 RFRFQGnandpdqngnNTQSPPSRDVSPTSrdnlvAKQLARNTVTQALSRFTS------PQAGASSRLGASPGGDAGTCP 519
Cdd:pfam03154 246 HPPLQP----------MTQPPPPSQVSPQP-----LPQPSLHGQMPPMPHSLQtgpshmQHPVPPQPFPLTPQSSQSQVP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 520 PVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASnagakvdnkiVASPPST-LPQGTKVVNEENVPKSSS 598
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPH----------IKPPPTTpIPQLPNPQSHKHPPHLSG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 599 PQ-------LPPKPSID-LTVASAGCPVSA--------LATSQVGAWPAETPGLNQ-PACTDSSLVIPTTVAFRS--SIN 659
Cdd:pfam03154 381 PSpfqmnsnLPPPPALKpLSSLSTHHPPSAhppplqlmPQSQQLPPPPAQPPVLTQsQSLPPPAASHPPTSGLHQvpSQS 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 660 PVSASSRSPGASDSLLvTASGWSPSLTPlLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLD 726
Cdd:pfam03154 461 PFPQHPFVPGGPPPIT-PPSGPPTSTSS-AMPGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALD 525
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
118-257 |
3.60e-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: 48.41 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQER------MSAQLAAAESRQKKLEME--------KLQLQALEQEHKKLAahlEEERgkNKHVVLMLVKE-----CK 178
Cdd:pfam15709 352 RKRREQeeqrrlQQEQLERAEKMREELELEqqrrfeeiRLRKQRLEEERQRQE---EEER--KQRLQLQAAQErarqqQE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 179 QLSGKVVE-EAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGM--EAQLEKQlfefdtEREQLRAKLTREEAHTTDLK 255
Cdd:pfam15709 427 EFRRKLQElQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQ------RQKQEAEEKARLEAEERRQK 500
|
..
gi 167555091 256 EE 257
Cdd:pfam15709 501 EE 502
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
800-825 |
3.95e-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: 41.80 E-value: 3.95e-05
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
135-249 |
4.53e-05 |
|
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: 44.50 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 135 QKKLEMEKLQLQALEQEHKKLaahleeergKNKHVVLML----VKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELED 210
Cdd:pfam18595 1 SSTLAEEKEELAELERKAREL---------QAKIDALQVvekdLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEEKEI 71
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 167555091 211 QLSAEKQRsagmEAQLEKQL--FEFDTEREQLRAKLTREEA 249
Cdd:pfam18595 72 ELRELERR----EERLQRQLenAQEKLERLREQAEEKREAA 108
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
742-820 |
4.75e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 4.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 742 AKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLL 820
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
127-258 |
5.00e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 127 QLAAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSgKVVEEAQKLEEvmvKLEEEKKK 204
Cdd:COG4372 27 AALSEQLRKALFELDKLQeeLEQLREELEQAREELEQLEEE-------LEQARSELE-QLEEELEELNE---QLQAAQAE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 167555091 205 TSELEDQLSAEKQRSAGMEAQLEKQLfefdTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-259 |
5.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 9 EPDLSRapgdaEGATAEAAKKEFDVDTLSKSELRMLLSVMEGELEARDLVIEALRARRKEVF-----IQERYGRFNLNDP 83
Cdd:PRK03918 216 LPELRE-----ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeieeLEEKVKELKELKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 84 flaLQRDYEAGAGDKEKpvctnplsiLEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLE--E 161
Cdd:PRK03918 291 ---KAEEYIKLSEFYEE---------YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 162 ERGKNKHVVLMLVKECKQLSGKVVEEaqKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGME---AQLEKQLFEF----- 233
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELkkakg 436
|
250 260 270
....*....|....*....|....*....|....*.
gi 167555091 234 ----------DTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:PRK03918 437 kcpvcgreltEEHRKELLEEYTAELKRIEKELKEIE 472
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
704-841 |
5.65e-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: 47.77 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 704 LQQAAAQGNVTLLSMLLNEEGLDInyccEDSHSALYSAAKNGHtDCVRLLLNAEARVDAADKN--------------GFT 769
Cdd:TIGR00870 56 LFVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAILLHLLAAFRKSGPlelandqytseftpGIT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 770 PLCVAAAQGHFECIELLTAYNANINHSAAG--------------GQTPLYLACKTGNKECIKLLLEAGTDrsIKTRD--G 833
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPAD--ILTADslG 208
|
....*...
gi 167555091 834 WTPIHAAV 841
Cdd:TIGR00870 209 NTLLHLLV 216
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
366-710 |
5.81e-05 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 47.65 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 366 PSPPTALP-SSASRIEENGPSAGNAPDLSN-STPSTPSGTAPAAAQTLGAAPQNHSQAPPVHSLHSPCA--NTHPGLNPR 441
Cdd:pfam17823 67 PAPVTLTKgTSAAHLNSTEVTAEHTPHGTDlSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAalPSEAFSAPR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 442 IQAARfrfqGNANDPDQNGNNTQSPPSRdVSPTSRDNLVAKQLARNTVTQALSRFTSPQAGASSRLGASPGGDA--GTCP 519
Cdd:pfam17823 147 AAACR----ANASAAPRAAIAAASAPHA-ASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAatATGH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 520 PVGRTGLKTPGAARVDRGNPPPIPPKKPGLSQTPSPPHPQLRASNAGAKVdnkiVASPPSTLPQGTKVVNEENVPKSSSP 599
Cdd:pfam17823 222 PAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTIN----MGDPHARRLSPAKHMPSDTMARNPAA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 600 QLPPKPSIDLTVASAGCPVSALATSQVGAWPAETPGLNQP---ACTDSSLVIPTTVAFR---SSINPVSASSRSPgasdS 673
Cdd:pfam17823 298 PMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPksvASTNLAVVTTTKAQAKepsASPVPVLHTSMIP----E 373
|
330 340 350
....*....|....*....|....*....|....*...
gi 167555091 674 LLVTASGWSPS-LTPLLMSGGPaplaGRPTLLQQAAAQ 710
Cdd:pfam17823 374 VEATSPTTQPSpLLPTQGAAGP----GILLAPEQVATE 407
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-259 |
5.92e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 8 CEPDLSRAPGDAEGATAEAAKKEFDVDTLSK--SELRMLLSVMEGELEARDLVIEALRARRKEvfIQERYG-----RFNL 80
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREeaAELESELEEAREAVEDRREEIEELEEEIEE--LRERFGdapvdLGNA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 81 NDpFLALQRDYEAGAGDKEKPvctnplsiLEAVMAHCRKMQERMSAQLAA-------------------AESRQKKLEME 141
Cdd:PRK02224 411 ED-FLEELREERDELREREAE--------LEATLRTARERVEEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 142 ------KLQLQALEQEHKKLAAHLEEERGKNKhvvlmlVKECKQLSGKVVEEAQ-KLEEVMVKLEEEKKKTSELEDQL-- 212
Cdd:PRK02224 482 aeledlEEEVEEVEERLERAEDLVEAEDRIER------LEERREDLEELIAERReTIEEKRERAEELRERAAELEAEAee 555
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 213 ---SAEKQRSAGMEAQ-----LEKQLFEFDTEREQLRaKLTREEAHTTDLKEEID 259
Cdd:PRK02224 556 kreAAAEAEEEAEEAReevaeLNSKLAELKERIESLE-RIRTLLAAIADAEDEIE 609
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
719-771 |
5.98e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 5.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167555091 719 LLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPL 771
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-249 |
6.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 11 DLSRAPGDAEgaTAEAAKKEFDVDtlSKSELRMLLSVMEGElEAR--DLVIEALRARRKEvfiQERygRFNLNDPFLALQ 88
Cdd:PTZ00121 1167 EEARKAEDAK--KAEAARKAEEVR--KAEELRKAEDARKAE-AARkaEEERKAEEARKAE---DAK--KAEAVKKAEEAK 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 89 RDYEAGAGDKEKPVCTNPLSILEAVMAHCRKMQERMSAqlaaaESRQKKLEMEKlqlqaleQEHKKLAAHLEEERGKNKh 168
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-----EEARKADELKK-------AEEKKKADEAKKAEEKKK- 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 169 vvlmlVKECKqlsgKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRA-KLTRE 247
Cdd:PTZ00121 1304 -----ADEAK----KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKE 1374
|
..
gi 167555091 248 EA 249
Cdd:PTZ00121 1375 EA 1376
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-257 |
7.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAH----LEEERGKNKHV--VLMLVKECKQLSGKVVEEAQKL 191
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakkAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKA 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 192 EEV--------------MVKLEEEKKKTSELEDQLSAEKQRsagmEAQLEKQLfEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:PTZ00121 1650 EELkkaeeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKKA----AEALKKEA-EEAKKAEELKKKEAEEKKKAEELKKA 1724
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
107-258 |
7.84e-05 |
|
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: 45.56 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 107 LSILEAVMAHCRKMQERMS---AQLAAAESRQKKLEMEKLQL--QALEQEHKKL-AAHLEEERGKNKHVVLMLVKECKQL 180
Cdd:pfam14662 7 LTCVEDLQANNQKLLQENSklkATVETREETNAKLLEENLNLrkQAKSQQQAVQkEKLLEEELEDLKLIVNSLEEARRSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 181 SGK---VVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:pfam14662 87 LAQnkqLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQIEELKST 166
|
.
gi 167555091 258 I 258
Cdd:pfam14662 167 V 167
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
40-246 |
8.26e-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: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 40 ELRMLLSVMEGELEARD--LVI---EALRARRKEVfIQERYgrfnlndpflALQRDYEAGAGDKEKPVCTNPLSILEAVM 114
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDmlLVVpraELLQNRLEEC-LQERA----------ELLQAQEAANRQREKEKERYKRDREQWER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 115 AHcRKMQERMS-AQLAAAESRQKKLEMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKL 191
Cdd:pfam07888 74 QR-RELESRVAeLKEELRQSREKHEELEEKYkeLSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 192 EEV---------MVKLEEEKKKTSELEDQLSAEKQRSAGMEAQ-LEKQLFEFDTEREQLRAKLTR 246
Cdd:pfam07888 153 ERMkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQeLRNSLAQRDTQVLQLQDTITT 217
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
380-708 |
8.42e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 380 EENGPSA-GNAPDLSNSTPSTPSgtapaaaqtlgAAPQNHSQAPPVHSLHSPCANTHPGLNPRIQAARFRFQGNANDPDQ 458
Cdd:PHA03247 2485 EARFPFAaGAAPDPGGGGPPDPD-----------APPAPSRLAPAILPDEPVGEPVHPRMLTWIRGLEELASDDAGDPPP 2553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 459 NGNNTQSPPSRDVS-PTSRdnlvakQLARNTVTQALSRFTSPQAGASSRLGASPGGDAG--------TCPPVGRTGLKTP 529
Cdd:PHA03247 2554 PLPPAAPPAAPDRSvPPPR------PAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGdprgpappSPLPPDTHAPDPP 2627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 530 GAARVDRGNPPPippkkpGLSQTPSPPHPQLRASNAGAKV------DNKIVASPPSTLPQGTK----------VVN---- 589
Cdd:PHA03247 2628 PPSPSPAANEPD------PHPPPTVPPPERPRDDPAPGRVsrprraRRLGRAAQASSPPQRPRrraarptvgsLTSladp 2701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 590 ------EENVPKSSSPQLPPKPSIDLTVASAGCPVSALATSQVGAWPAETPGLNQPAC--TDSSLVIPTTVAFRSSiNPV 661
Cdd:PHA03247 2702 ppppptPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPAPAPPAAPAA-GPP 2780
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 662 SASSRSPGASDSLLVTA--SGWSPSLTPLLMSG---------GPAPLAGRPTLLQQAA 708
Cdd:PHA03247 2781 RRLTRPAVASLSESRESlpSPWDPADPPAAVLApaaalppaaSPAGPLPPPTSAQPTA 2838
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-258 |
8.79e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 136 KKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSae 215
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-- 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 167555091 216 kqrsagmeaQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:COG4372 84 ---------ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-259 |
8.97e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 19 AEGATAEAAKKEFDvDTLSK--SELRMLLSVMEGELEARDL--VIEALRArrkevfIQERYGRFNLNDpflaLQRDYEAG 94
Cdd:PRK03918 459 AELKRIEKELKEIE-EKERKlrKELRELEKVLKKESELIKLkeLAEQLKE------LEEKLKKYNLEE----LEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 95 AGDKEKpvctnplsileavMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEE------------- 161
Cdd:PRK03918 528 EKLKEK-------------LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerl 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 162 ---ERGKNKHVVLM--------LVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGME-AQLEKQ 229
Cdd:PRK03918 595 kelEPFYNEYLELKdaekelerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEyLELSRE 674
|
250 260 270
....*....|....*....|....*....|
gi 167555091 230 LFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
25-258 |
9.29e-05 |
|
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: 47.26 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 25 EAAKKEFDvdtlskSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERygrfnlndpflalQRDYEAGAGDKEKPVCT 104
Cdd:COG5185 328 EESKRETE------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-------------LSKSSEELDSFKDTIES 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 105 NPLSILEAVMAHCRKMQE---RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKEckqls 181
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEilaTLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS----- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 182 gKVVEEAQKLE-EVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLT-----REEAHTTDLK 255
Cdd:COG5185 464 -RLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKdfmraRGYAHILALE 542
|
...
gi 167555091 256 EEI 258
Cdd:COG5185 543 NLI 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-259 |
1.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 109 ILEAVMAHCRKMQErMSAQLAAAES---------RQKKLEMEKLQLQALEQEHKKLAAH---LEEERGKNKHVVLMLVKE 176
Cdd:COG4913 253 LLEPIRELAERYAA-ARERLAELEYlraalrlwfAQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 177 CKQLSGKVVEEAQK-LEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFE-------FDTEREQLRAKLTREE 248
Cdd:COG4913 332 IRGNGGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalleaLEEELEALEEALAEAE 411
|
170
....*....|.
gi 167555091 249 AHTTDLKEEID 259
Cdd:COG4913 412 AALRDLRRELR 422
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-258 |
1.10e-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: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 121 QERMSA---QLAAAESRQKKLEMEklqLQALEQEHKKLAAH---LEEERgknkHVVLMLVKECKQLSGKVVEEAQKLEEV 194
Cdd:pfam01576 4 EEEMQAkeeELQKVKERQQKAESE---LKELEKKHQQLCEEknaLQEQL----QAETELCAEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167555091 195 MVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI 140
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
833-921 |
1.11e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 833 GWTPIHAAVDTGNVDSLKLLMYHRVPapgnslsaeepksglfslnggesppgsskpvvpadlINHADKEGWTAAHIAASK 912
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD------------------------------------INAVDGNGETALHFAASN 44
|
....*....
gi 167555091 913 GFKNCLEIL 921
Cdd:pfam13637 45 GNVEVLKLL 53
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
73-224 |
1.20e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 73 ERYGRfnlndpflalQRDYEAGAGDKEKPvctnplsileavmahcRKMQERMSAQ-----LAAAESRQKKLEMEKLQLQA 147
Cdd:PRK09510 62 EQYNR----------QQQQQKSAKRAEEQ----------------RKKKEQQQAEelqqkQAAEQERLKQLEKERLAAQE 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 148 lEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLsgKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEA 224
Cdd:PRK09510 116 -QKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA--KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEA 189
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
144-243 |
1.26e-04 |
|
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: 46.87 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 144 QLQALEQEHKKLaahleEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKktsELEDQLSAEKQRSAGME 223
Cdd:COG3096 513 RLQQLRAQLAEL-----EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE---ELEEQAAEAVEQRSELR 584
|
90 100
....*....|....*....|
gi 167555091 224 AQLEkqlfEFDTEREQLRAK 243
Cdd:COG3096 585 QQLE----QLRARIKELAAR 600
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-257 |
1.29e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 122 ERMSAQLAAA--ESRQKKLEMEKLQLQALEQEHKKLAAHLEEERgknkhvvlmlvKECKQLSGKVVEEAQKLEEVMVKLE 199
Cdd:COG1196 223 KELEAELLLLklRELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 200 EEKKKTSELEDQLSAEKQRSAGMEAQLEKqlfefdtEREQLRAKLTREEAHTTDLKEE 257
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEE-------LEEELAELEEELEELEEELEEL 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
118-258 |
1.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKLEMEKLqLQALEQEHKKLAAHLEEERGKNKHVvlmlvkecKQLSGKVVEEAQKLEEvmvK 197
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNEL--------QKLEKRLLQKEENLDR---K 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 198 LEEEKKKTSELEDQLSAEKQRsagmEAQLEKQLFEFDTEREQLRAKL------TREEAhttdlKEEI 258
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQK----QQELEKKEEELEELIEEQLQELerisglTAEEA-----KEIL 159
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-320 |
1.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQE---RMSAQLAAAESRQKKLEmeklQLQALEQEHKKLAAHLEEERGKNKHVVlmlvkecKQLSGKVVEEAQKLEEV 194
Cdd:PTZ00121 1681 KKAEEdekKAAEALKKEAEEAKKAE----ELKKKEAEEKKKAEELKKAEEENKIKA-------EEAKKEAEEDKKKAEEA 1749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 195 MVKlEEEKKKTSEL--EDQLSAEKQRSAGmEAQLEKQLfefDTEREQLRAKLTREEAHTTDLKEEIdkmkkmmeqMKKGN 272
Cdd:PTZ00121 1750 KKD-EEEKKKIAHLkkEEEKKAEEIRKEK-EAVIEEEL---DEEDEKRRMEVDKKIKDIFDNFANI---------IEGGK 1815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167555091 273 DGKPGLSLPRKTKDKRlasisvategpvTRSVACQTDVVTESTDPVKK 320
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSA------------IKEVADSKNMQLEEADAFEK 1851
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
800-831 |
1.81e-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: 40.35 E-value: 1.81e-04
10 20 30
....*....|....*....|....*....|...
gi 167555091 800 GQTPLYLAC-KTGNKECIKLLLEAGTDRSIKTR 831
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
40-244 |
1.94e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 40 ELRMLLSVME---GELEA--------RDLVIEALRARRKE---------VFIQERYGRFNLNDPFLALQRDYEAGAGDKE 99
Cdd:pfam19220 7 LLRVRLGEMAdrlEDLRSlkadfsqlIEPIEAILRELPQAksrlleleaLLAQERAAYGKLRRELAGLTRRLSAAEGELE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 100 KPVC-----TNPLSILEAVMAHCRKMQERMSAQLAAAEsRQKKLEMEklQLQALEQEHK----------KLAAHLEEERG 164
Cdd:pfam19220 87 ELVArlaklEAALREAEAAKEELRIELRDKTAQAEALE-RQLAAETE--QNRALEEENKalreeaqaaeKALQRAEGELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 165 KNKHVVLMLVKECKQL-------SGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTER 237
Cdd:pfam19220 164 TARERLALLEQENRRLqalseeqAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAER 243
|
....*..
gi 167555091 238 EQLRAKL 244
Cdd:pfam19220 244 ASLRMKL 250
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
118-243 |
2.14e-04 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 43.88 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQlaaaeSRQKKLeMEKLQLQALEQ-------EHKKLAAHLEEERGKNKHVVLMLVKECKQLSGkvvEEAQK 190
Cdd:pfam15035 2 RKLQAYQEAQ-----QRQAQL-VQKLQAKVLQYkkrcselEQQLLEKTSELEKTELLLRKLTLEPRLQRLER---EHSAD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 191 LEEVMVKLEEEKKKTSE-------LEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAK 243
Cdd:pfam15035 73 LEEALIRLEEERQRSESlsqvnslLREQLEQASRANEALREDLQKLTNDWERAREELEQK 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-245 |
2.41e-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: 46.20 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 22 ATAEAAKKEFDVDTL--SKSELRMLLSVMEGELEArdLVIEALRARRKEVFIQERygRFNLNDPFLALQRDYEAgagDKE 99
Cdd:TIGR02168 258 LTAELQELEEKLEELrlEVSELEEEIEELQKELYA--LANEISRLEQQKQILRER--LANLERQLEELEAQLEE---LES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 100 KPVC--------TNPLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAAHLEEERGKNKHVVL 171
Cdd:TIGR02168 331 KLDElaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELE------EQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 172 M------LVKECKQLSGKVVEEAQKLEEVMVK------------LEEEKKKTSELEDQLSAEKQRsagmEAQLEKQLFEF 233
Cdd:TIGR02168 405 LearlerLEDRRERLQQEIEELLKKLEEAELKelqaeleeleeeLEELQEELERLEEALEELREE----LEEAEQALDAA 480
|
250
....*....|..
gi 167555091 234 DTEREQLRAKLT 245
Cdd:TIGR02168 481 ERELAQLQARLD 492
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-425 |
2.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 126 AQLAAAESRQKKL--EMEKLQ--LQALEQEHKKLAAHLEEERGKNKHVVLML-----------VKECKQLSGKVVEEAQK 190
Cdd:COG3883 58 AELEALQAEIDKLqaEIAEAEaeIEERREELGERARALYRSGGSVSYLDVLLgsesfsdfldrLSALSKIADADADLLEE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 191 LEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEIDKMKKMMEQMKK 270
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 271 GNDGKPGLSLPRKTKDKRLASISVATEGPVTRSVACQTDVVTEStdpvkklPLSVPIKPSTGSPLVSTNTKGNVGPSALL 350
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS-------AGAAGAAAGAAGAGAAAASAAGGGAGGAG 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 351 IRPGIDRQASHSDLGPSPPTALPSSASRIEENGPSAGNAPDLSNSTPSTPSGTAPAAAQTLGAAPQNHSQAPPVH 425
Cdd:COG3883 291 GGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGGGG 365
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
766-794 |
2.68e-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: 39.49 E-value: 2.68e-04
10 20
....*....|....*....|....*....
gi 167555091 766 NGFTPLCVAAAQGHFECIELLTAYNANIN 794
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
132-257 |
4.97e-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: 42.37 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 132 ESRQKKLEMEKLQLQAlEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQ-KLEEVMVKLEEEKKKTSELED 210
Cdd:pfam11600 5 KSVQSQEEKEKQRLEK-DKERLRRQLKLEAEKEEKER----LKEEAKAEKERAKEEARrKKEEEKELKEKERREKKEKDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 167555091 211 QLSAEKQRsAGMEAQLEKQlfefdterEQLRAKL--TREEAHTTDLKEE 257
Cdd:pfam11600 80 KEKAEKLR-LKEEKRKEKQ--------EALEAKLeeKRKKEEEKRLKEE 119
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
703-916 |
5.13e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.66 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 703 LLQQAAAQGNVTLLSMLLNEEGLDINYCCE-------------DSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFT 769
Cdd:PHA02946 28 MLQAIEPSGNYHILHAYCGIKGLDERFVEEllhrgyspnetddDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 770 PLCVAAAQGH--FECIELLTAYNANINHSA-AGGQTPLyLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHaavdtgnv 846
Cdd:PHA02946 108 PLYYLSGTDDevIERINLLVQYGAKINNSVdEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-------- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 847 dslkllmyhrvpapgNSLSAEEPKSGLFS--LNGGESPpgsSKPvvpadlinhaDKEGWTAAHIAASKGFKN 916
Cdd:PHA02946 179 ---------------RHLMSDNPKASTISwmMKLGISP---SKP----------DHDGNTPLHIVCSKTVKN 222
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-254 |
5.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 126 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---HLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMVKLEEeK 202
Cdd:COG4913 668 REIAELEAELERLDASSDDLAALEEQLEELEAeleELEEELDE-------LKGEIGRLEKELEQAEEELDELQDRLEA-A 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 167555091 203 KKTSELEDQLSAEKQRSAGMEAQLEKQLFE-FDTEREQLRAKLTREEAHTTDL 254
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERA 792
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-259 |
5.83e-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: 44.78 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 9 EPDLSRAPGDAEGATAEAAKKEFDVDTLSKSELRMllsvmEGELEarDLVIEALRARRKEVFIQERYGRFnlnDPFLAlq 88
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL-----QQELD--DLLVDLDHQRQLVSNLEKKQKKF---DQMLA-- 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 89 rdyeagagdKEKpvctnplsileavMAHCRKMQERMSAQlaaAESRQKK---------LEMEKLQLQALEQEHKKLAAHL 159
Cdd:pfam01576 612 ---------EEK-------------AISARYAEERDRAE---AEAREKEtralslaraLEEALEAKEELERTNKQLRAEM 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 160 EEergknkhvvlmLVKEcKQLSGKVVEEAQKLEEVM-VKLEEEKKKTSELEDQLSA-------------------EKQRS 219
Cdd:pfam01576 667 ED-----------LVSS-KDDVGKNVHELERSKRALeQQVEEMKTQLEELEDELQAtedaklrlevnmqalkaqfERDLQ 734
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 167555091 220 AGMEA------QLEKQLFEFDTEREQLRAKltREEAHTTDLKEEID 259
Cdd:pfam01576 735 ARDEQgeekrrQLVKQVRELEAELEDERKQ--RAQAVAAKKKLELD 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-258 |
6.92e-04 |
|
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: 44.24 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 137 KLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGK--VVEEAQK---------------LEEVMVKLE 199
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKttEISNTQTqlnqlkdeqnkikkqLSEKQKELE 277
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 200 EEKKKTSELEDQLSA--------EKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEI 258
Cdd:TIGR04523 278 QNNKKIKELEKQLNQlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
105-249 |
6.94e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 105 NPLSILEAVMahcRKMQE---RMSAQLAAAESRQKKLEMeklQLQALEQEHKKLaahleEERgknkhVVLMLVKECKQLS 181
Cdd:COG1842 23 DPEKMLDQAI---RDMEEdlvEARQALAQVIANQKRLER---QLEELEAEAEKW-----EEK-----ARLALEKGREDLA 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 182 GKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQrsagmeaQLEKQLFEFDTEREQLRAKLTREEA 249
Cdd:COG1842 87 REALERKAELEAQAEALEAQLAQLEEQVEKLKEALR-------QLESKLEELKAKKDTLKARAKAAKA 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-259 |
7.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 126 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHvVLMLVKECKQLSGkVVEEAQKLEEVMVKLEEEKKKT 205
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVAS-AEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 167555091 206 SELEDQLSAEKQRsagmEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:COG4913 688 AALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
121-241 |
7.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 121 QERMSAQLAAAESRQKKLEmekLQLQALEQEHKKLAA---HLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVK 197
Cdd:COG4372 96 LAQAQEELESLQEEAEELQ---EELEELQKERQDLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 167555091 198 LEEEKKKTSELE-DQLSAEKQRSAGMEAQLEKQLFEFDTEREQLR 241
Cdd:COG4372 173 LQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELA 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-231 |
7.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 59 IEALRARRKEvfIQERYGRFN-LNDPFLALQRDYEAGAGDKEKpvCTNPLSILEAVMAHCRKMQERMSA--QLAAAESRQ 135
Cdd:COG4717 73 LKELEEELKE--AEEKEEEYAeLQEELEELEEELEELEAELEE--LREELEKLEKLLQLLPLYQELEALeaELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 136 KKLEMEKL-------QLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSEL 208
Cdd:COG4717 149 EELEERLEelreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180
....*....|....*....|...
gi 167555091 209 EDQLSAEKQRSAgMEAQLEKQLF 231
Cdd:COG4717 229 LEQLENELEAAA-LEERLKEARL 250
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
736-913 |
8.80e-04 |
|
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: 44.10 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 736 SALYSAA---KNGHTDCVRLLLNAEARVDAADK-----------NGFTPLCVAAAQGHFECIELLTAYNANINHSAAG-- 799
Cdd:cd21882 28 TCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGrf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 800 -----------GQTPLYLACKTGNKECIKLLLEAGTD-RSIKTRD--GWTPIHAAVDTGNvdslkllmyhrvPAPGNSLS 865
Cdd:cd21882 108 frkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpAALEAQDslGNTVLHALVLQAD------------NTPENSAF 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167555091 866 AEEPKSGLFSLNggesppGSSKPVVPADLI-NHadkEGWTAAHIAASKG 913
Cdd:cd21882 176 VCQMYNLLLSYG------AHLDPTQQLEEIpNH---QGLTPLKLAAVEG 215
|
|
| PHA02917 |
PHA02917 |
ankyrin-like protein; Provisional |
783-856 |
1.11e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165231 [Multi-domain] Cd Length: 661 Bit Score: 43.83 E-value: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 783 IELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAV-DTGNVDSLKLLMYHR 856
Cdd:PHA02917 435 INICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLLCHK 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
118-258 |
1.15e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAE--------SRQKKLEMEKLQLQALE--QEH-----KKLAAHLEEERGKNkhvvLMLVKECKQLS- 181
Cdd:pfam05483 424 KKQFEKIAEELKGKEqelifllqAREKEIHDLEIQLTAIKtsEEHylkevEDLKTELEKEKLKN----IELTAHCDKLLl 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 182 --GKVVEEAQKLEEVMVKLEEE----KKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLK 255
Cdd:pfam05483 500 enKELTQEASDMTLELKKHQEDiincKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIE 579
|
...
gi 167555091 256 EEI 258
Cdd:pfam05483 580 YEV 582
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
771-853 |
1.16e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.44 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 771 LCVAAAQGHFECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNVDSLK 850
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
...
gi 167555091 851 LLM 853
Cdd:PHA02875 86 ELL 88
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
707-1000 |
1.24e-03 |
|
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: 43.59 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 707 AAAQGNVTLLSMLLNeegldINYCCEDSHSALYSAAKNghTDCVRLLLNAEarVDAADKNGFTPLCVAAAQGHFECIELL 786
Cdd:cd22194 90 ASDTGKTCLMKALLN-----INENTKEIVRILLAFAEE--NGILDRFINAE--YTEEAYEGQTALNIAIERRQGDIVKLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 787 TAYNANINHSAAG--------------GQTPLYLACKTGNKECIKLLLEAG-TDRSIKTRDGWTPIHAAV----DTGNVD 847
Cdd:cd22194 161 IAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaeDSKTQN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 848 SLKLLMYHRVpapgnsLSAEEPKSglfslnggesppgsskpvvpadLINHADKEGWTAAHIAASKGfknCLEILcrHGGL 927
Cdd:cd22194 241 DFVKRMYDMI------LLKSENKN----------------------LETIRNNEGLTPLQLAAKMG---KAEIL--KYIL 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 928 EPERRDKCNRTVHDVATD-----DCKHLLEnLNALKIPLRISVGEIQPSNDGSDDFECEHTICTLNIRKQTSWEDFSK 1000
Cdd:cd22194 288 SREIKEKPNRSLSRKFTDwaygpVSSSLYD-LTNVDTTTDNSVLEIIVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAR 364
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
703-938 |
1.29e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.51 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 703 LLQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFEC 782
Cdd:PHA02876 148 LIKERIQQDELLIAEMLL-EGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 783 IELLTAYNANINHSaaggQTPLYLACKTGNKECIKLLLEAGTdrSIKTRDGW--TPIHAAVDTGNVDSLKLLMYHR-VPA 859
Cdd:PHA02876 227 IKAIIDNRSNINKN----DLSLLKAIRNEDLETSLLLYDAGF--SVNSIDDCknTPLHHASQAPSLSRLVPKLLERgADV 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167555091 860 PGNSLSAEEPKSgLFSLNGGESPPGSSKPVVPADlINHADKEGWTAAHIAASKGFKNCLEILCRHGGLEPERRDKCNRT 938
Cdd:PHA02876 301 NAKNIKGETPLY-LMAKNGYDTENIRTLIMLGAD-VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKT 377
|
|
| bZIP |
cd14686 |
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
118-167 |
1.34e-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: 38.30 E-value: 1.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167555091 118 RKMQERMSAQlaaaESRQ-KKLEMEKL--QLQALEQEHKKLAAHLEEERGKNK 167
Cdd:cd14686 4 RRERNREAAR----RSRErKKERIEELeeEVEELEEENEELKAELEELRAEVE 52
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-259 |
1.35e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 9 EPDLSRAPGDAEGATAEAAKKEFDVDTLS--KSELRMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRF-NLNDPFL 85
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 86 ALQ---RDYEAGAGDKEKPvcTNPLSILEAVMAHCRK-MQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAA---H 158
Cdd:TIGR02169 802 KLEeevSRIEARLREIEQK--LNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAalrD 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 159 LEEERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLS-----------------------AE 215
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvqAE 959
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 216 KQRsagMEAQLEK---------QLFEFDTER----EQLRAKLTREEAHTTDLKEEID 259
Cdd:TIGR02169 960 LQR---VEEEIRAlepvnmlaiQEYEEVLKRldelKEKRAKLEEERKAILERIEEYE 1013
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
107-259 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 107 LSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEklqLQALEQEHK-KLAAHLEEERGKNKHvvlmlvkeckqlsgkvv 185
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE---LEALTQQLEeKAAAYDKLEKTKNRL----------------- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 186 eeAQKLEEVMVKLEEEKKKTSELE------DQLSAEkQRSAGMEAQLEKQLFEFDTEREQLRA-KLTREEAHTTDLKEEI 258
Cdd:pfam01576 579 --QQELDDLLVDLDHQRQLVSNLEkkqkkfDQMLAE-EKAISARYAEERDRAEAEAREKETRAlSLARALEEALEAKEEL 655
|
.
gi 167555091 259 D 259
Cdd:pfam01576 656 E 656
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
124-256 |
1.43e-03 |
|
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: 41.81 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 124 MSAQLAA--AESR--QKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVlMLVKEcKQLSGKvvEEAQ-KLEEVMVKL 198
Cdd:pfam15619 58 LPQLIARhnEEVRvlRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLE-KLSED-KNLAER--EELQkKLEQLEAKL 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167555091 199 EEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEahtTDLKE 256
Cdd:pfam15619 134 EDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQ---QKLKE 188
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-290 |
1.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 111 EAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQ--EHKKLAAHLEEERGKNKHVVLMLVKecKQLSGKVVEEA 188
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 189 QKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKltREEAHTTD-LKEEIDKMKKMMEQ 267
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADeAKKKAEEAKKKADE 1501
|
170 180
....*....|....*....|...
gi 167555091 268 MKKGNDGKPGLSLPRKTKDKRLA 290
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKA 1524
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-253 |
1.51e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKLEM----EKLQLQAlEQEHKKLAAHLEEergKNKHVVLM---------LVKECKQLSGKV 184
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELraelKELRKEA-EEIHKKIKELAEE---AQELHEEMielykeadeLRKEADELHKEI 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167555091 185 VEEAQKLEEVMVKLEEEKKKTSELEDQLSA--EKQRSAGMEAQlEKQLFEfdtEREQLRAKLTREEAHTTD 253
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKlrKKQRALKREKE-KEELEE---KAEEIFEKLKKGEKLTTE 285
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
135-259 |
1.52e-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: 43.47 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 135 QKKLEMEKL---------QLQALEQEHKKLAAHLEE---ERGKNKHVVLMLVKECKQLSGKVVEEAQKLEEVMVKLEEEK 202
Cdd:TIGR04523 451 VKELIIKNLdntresletQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 203 KKTSELEDQLSaekqrsagmeaQLEKQLFEFDTEreqlrakLTREEahttdLKEEID 259
Cdd:TIGR04523 531 SEKKEKESKIS-----------DLEDELNKDDFE-------LKKEN-----LEKEID 564
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
118-232 |
1.65e-03 |
|
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: 39.86 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEhkklaahLEEERGKNKhvvlMLVKECKQLSGKVVEEAQKLEEVMVK 197
Cdd:pfam13863 9 FLVQLALDAKREEIERLEELLKQREEELEKKEQE-------LKEDLIKFD----KFLKENDAKRRRALKKAEEETKLKKE 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 167555091 198 LEEEKKKtseLEDQLSAEKQRSAGMEAQLEK-QLFE 232
Cdd:pfam13863 78 KEKEIKK---LTAQIEELKSEISKLEEKLEEyKPYE 110
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
719-795 |
1.70e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 42.73 E-value: 1.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 719 LLNEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLTAYNANINH 795
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
365-520 |
1.85e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 365 GPSPPTALPSSASRIEENGPSAGNAPdlsnSTPSTPSGTAPAAAQTLGAAPQNHSQAPPVHSlHSPCANTHPGLNPRIQA 444
Cdd:PRK07764 596 GGEGPPAPASSGPPEEAARPAAPAAP----AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHH-PKHVAVPDASDGGDGWP 670
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 445 ARFRFQGNANDPDQNGNNTQSPPSRDVSPTSrdnlVAKQLARNTVTQALSRFTSPQAGASSRLGASPGGDAGTCPP 520
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQP----APAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLP 742
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
129-243 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 129 AAAESRQKKLEMEKLQLQALEQEH---KKLA-----------AHLEEERGKNKHVVLMLVKECKQLSGKVVEEAQklEEV 194
Cdd:pfam13904 63 AKQRQRQKELQAQKEEREKEEQEAelrKRLAkekyqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEA 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167555091 195 MVKLEE-EKKKTSELEDQlsAEKQRSAGMEAQLEKQlfefdtEREQLRAK 243
Cdd:pfam13904 141 KEVLQEwERKKLEQQQRK--REEEQREQLKKEEEEQ------ERKQLAEK 182
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
703-771 |
2.05e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.93 E-value: 2.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 703 LLQQAAAQGNVTLLSMLLnEEGLDINYCCEDSHSALYSAAKNGHTDCVRLLLNAEARVDAAD-KNGFTPL 771
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
317-634 |
2.06e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.83 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 317 PVKKLPLSVPIKPSTGSPLVSTNTKGNV--GPSALLIRP------------GIDRQASHSDLGPSPPTALPSSASRIEEN 382
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLPQPSLHGQMppMPHSLQTGPshmqhpvppqpfPLTPQSSQSQVPPGPSPAAPGQSQQRIHT 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 383 GPSAgnapdlsnstpSTPSGTAPAAAQTLGAAPQN--HSQAPP---VHSLHSPCANTHPglnPRIQAARfRFQGNANDPd 457
Cdd:pfam03154 328 PPSQ-----------SQLQSQQPPREQPLPPAPLSmpHIKPPPttpIPQLPNPQSHKHP---PHLSGPS-PFQMNSNLP- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 458 qngnntqSPPSrdVSPTSrdnlvakqlarntvtqALSRFTSPQAGASSrLGASPGGDAGTCPPVGRTGLKTPGAARVDRG 537
Cdd:pfam03154 392 -------PPPA--LKPLS----------------SLSTHHPPSAHPPP-LQLMPQSQQLPPPPAQPPVLTQSQSLPPPAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 538 NPPPIPPKKPGLSQTPSPPHPqlrasnagakvdnKIVASPPSTLPQGTKVVNEENVPKSSSPQLPPKPSIDLTV-ASAGC 616
Cdd:pfam03154 446 SHPPTSGLHQVPSQSPFPQHP-------------FVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVpAAVSC 512
|
330
....*....|....*...
gi 167555091 617 PVSALATSQVGAWPAETP 634
Cdd:pfam03154 513 PLPPVQIKEEALDEAEEP 530
|
|
| LUC7 |
pfam03194 |
LUC7 N_terminus; This family contains the N terminal region of several LUC7 protein homologs ... |
111-230 |
2.09e-03 |
|
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: 41.82 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 111 EAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHkklAAHLEEERGKnkhvvlmLVKECKQL--SGKVvEEA 188
Cdd:pfam03194 83 REFLRFLQKLIDDVDRKIRKGKQRLELTQEEIEQTDELKQEQ---ISVLEEKIKK-------LLEEAEELgeEGNV-DEA 151
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 167555091 189 QKLeevMVKLEEEKKKTSELEDQLsaEKQRSAGMEAQlEKQL 230
Cdd:pfam03194 152 QKL---MKKVEELKEEKEELEQQY--ESLTKESAASQ-EKKM 187
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
766-794 |
2.10e-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. 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: 37.27 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|
gi 167555091 766 NGFTPLCVAAAQ-GHFECIELLTAYNANIN 794
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
121-244 |
2.10e-03 |
|
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: 39.93 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 121 QERMSAQLAAAESRQKKLeMEKLQLQAleqehkKLAAHLEE--ERGKNKHVvlmlvkeckqlsgkvvEEAQKLEEVMVKL 198
Cdd:pfam07926 10 IKRLKEEAADAEAQLQKL-QEDLEKQA------EIAREAQQnyERELVLHA----------------EDIKALQALREEL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 167555091 199 EEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKL 244
Cdd:pfam07926 67 NELKAEIAELKAEAESAKAELEESEESWEEQKKELEKELSELEKRI 112
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
132-249 |
2.73e-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: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 132 ESRQKKLEMEKLQLQALEQEHKKLAAHLEE-ERGKNKhvvlmLVKECKQLSGkVVEEAQKLEEVMvkleeeKKKTSELED 210
Cdd:pfam05010 57 EEKQKQKELEHAEIQKVLEEKDQALADLNSvEKSFSD-----LFKRYEKQKE-VISGYKKNEESL------KKCAQDYLA 124
|
90 100 110
....*....|....*....|....*....|....*....
gi 167555091 211 QLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEA 249
Cdd:pfam05010 125 RIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAETA 163
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
42-256 |
2.76e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 42.27 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 42 RMLLSVMEGELEA-------RDLVIEALRARRKEVFIQ---ERYGRFNLNDPfLALQRDYEAGAGDKEKpVCTNPLSILE 111
Cdd:pfam14643 151 KLFANLMEAELKQelsfrlrWQDRVDRWKALKTEHLIQefkEFIASEEIQNP-PERKKELEEMLKEQKK-LQQKRLELLQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 112 AV----MAHCRKMQerMSAQLAAAESRQKKLE------MEKLQ----------LQALEQEHKKL--AAHLEEERGKNkhv 169
Cdd:pfam14643 229 KIsdllPPAYSKSK--VEEWWASLEALNEQLDqyhdqcMTKLRaeyeevwqecLARVQKLKQELldYKVCSEEEAEA--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 170 vlMLVKECKQLSGKVVEEAQKLEEVMVKLEEEKKKtsELEDQLSAEK-------QRSAGMEAQLEKQLFEFDTEREQLRA 242
Cdd:pfam14643 304 --LVNEEFLPLVGKLQRDAEDELEKLDKFLEELAK--QTEAQSEDLFkffreaaQLWDVHQTELAKQELELEKKLEQCRQ 379
|
250 260 270
....*....|....*....|....*....|.
gi 167555091 243 KLT-----------------REEAHTTDLKE 256
Cdd:pfam14643 380 KHDqenqakeaaldkkldqlRQASTEEKLKE 410
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
180-259 |
2.98e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 180 LSGKVVEEAQ---------------KLEEVMVKLEEEKKKTSELEDQLSAEKQRsagmeaqLEKQLFEFDTEREQLRAKL 244
Cdd:COG1193 497 LPEEIIERARellgeesidveklieELERERRELEEEREEAERLREELEKLREE-------LEEKLEELEEEKEEILEKA 569
|
90
....*....|....*..
gi 167555091 245 tREEAHT--TDLKEEID 259
Cdd:COG1193 570 -REEAEEilREARKEAE 585
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-259 |
3.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 118 RKMQERMSAQLAAAESRQKKlEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmlVKECKqlsgKVVEEAQKLEEVMVK 197
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--------ADEAK----KKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 198 LEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAkltrEEAHTTDLKEEID 259
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA----DEAKKAEEKKKAD 1549
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
110-257 |
3.10e-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: 40.82 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 110 LEAVMAHCRKMQERMSAQLAAAESRQKKLEmeklqlQALEQEHKKLAAHLEEERGKNKHvvlmLVKECKQLSGKVVEEAQ 189
Cdd:pfam04012 45 LAQTIARQKQLERRLEQQTEQAKKLEEKAQ------AALTKGNEELAREALAEKKSLEK----QAEALETQLAQQRSAVE 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 190 KLEEVMVKLEeekKKTSELEDQLSAEKQR--SAGMEAQLEKQLFEFDTER-----EQLRAKLTREEAhTTDLKEE 257
Cdd:pfam04012 115 QLRKQLAALE---TKIQQLKAKKNLLKARlkAAKAQEAVQTSLGSLSTSSatdsfERIEEKIEEREA-RADAAAE 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
119-256 |
3.53e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 119 KMQ---ERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAhlEEERGKnkhvvLMLVKECKQLSgkvvEEAQKLEEvm 195
Cdd:pfam01576 437 KLQselESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ--EETRQK-----LNLSTRLRQLE----DERNSLQE-- 503
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 196 vKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTeREQLRAKLTRE-EAHTTDLKE 256
Cdd:pfam01576 504 -QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRElEALTQQLEE 563
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
744-841 |
3.63e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain] Cd Length: 607 Bit Score: 42.09 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 744 NGHTDCVRLLLNAEARVDAADK-----------NGFTPLCVAAAQGHFECIELLTAYNANINHSAAG------------- 799
Cdd:cd22193 42 PGTNDTIRILLDIAEKTDNLKRfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfy 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 167555091 800 -GQTPLYLACKTGNKECIKLLLE-AGTDRSIKTRD--GWTPIHAAV 841
Cdd:cd22193 122 fGELPLSLAACTNQPDIVQYLLEnEHQPADIEAQDsrGNTVLHALV 167
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
126-259 |
3.99e-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: 38.92 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 126 AQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHV---VLMLVKECKQLSGKVVEEAQKleevmvkleeEK 202
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELeaeVKKLEEALKKLKAELSEEKQK----------EK 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 203 KKTSELEDQLSaekqrsagMEAQLEKQlfefdteREQLRAKLtreEAHTTDLKEEID 259
Cdd:pfam04871 71 EKQSELDDLLL--------LLGDLEEK-------VEKYKARL---KELGEEVLSDDE 109
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
780-846 |
4.15e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.52 E-value: 4.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167555091 780 FECIELLTAYNANINHSAAGGQTPLYLACKTGNKECIKLLLEAGTDRSIKTRDGWTPIHAAVDTGNV 846
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSV 267
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
111-254 |
4.48e-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: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 111 EAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHlEEERGKNKhvvlmlvkecKQLSGKVVEEAQK 190
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-KKQMEKDN----------SELELKMEKVFQG 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 191 LEEVMVKLEEEKKKTSELEDQLSAEKQRSAG---MEAQL---EKQLFEFDTEREQLRAKLTREEAHTTDL 254
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEklnKERRLlnqEKTELLVEQGRLQLQADRHQEHIRARDS 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-230 |
4.48e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 124 MSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKnkhvvlmLVKECKQLSGKVVEEAQKLEEVMVKLEEEKK 203
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA-------LLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100
....*....|....*....|....*..
gi 167555091 204 KTSELEDQLSAEKQRSAGMEAQLEKQL 230
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELL 110
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
121-230 |
4.51e-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: 41.48 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 121 QERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQLSGKVVEEaqKLEEVMVKLEE 200
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEYQRQKQEA 486
|
90 100 110
....*....|....*....|....*....|..
gi 167555091 201 EKKKTSELED--QLSAEKQRSAGMEAQLEKQL 230
Cdd:pfam15709 487 EEKARLEAEErrQKEEEAARLALEEAMKQAQE 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-230 |
4.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 18 DAEGATAEAAKKEFDVDTLSKSELRMLLSVM--EGELEARDLVIEALRARRKEVFIQErygrfnlndpfLALQRDYEAGA 95
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEeaEEELEEAEAELAEAEEALLEAEAEL-----------AEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 96 GDKEKP-----VCTNPLSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKhvv 170
Cdd:COG1196 386 EELLEAlraaaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL--- 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 171 lmlvkecKQLSGKVVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQL 230
Cdd:COG1196 463 -------ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
123-257 |
4.57e-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: 39.21 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 123 RMSAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVvlmlvkEckqlsgkvvEEAQKLEEvmvKLEEEK 202
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQL------E---------EEVEKLEE---QLKEAK 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 167555091 203 KKTSEledqlsAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEE 257
Cdd:pfam12718 63 EKAEE------SEKLKTNNENLTRKIQLLEEELEESDKRLKETTEKLRETDVKAE 111
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
74-259 |
6.42e-03 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 40.72 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 74 RYGRFNLNDPFLALQRDYEAGAGDKEKPVCTN-------PlSILEAVMAHCRKMQERMSAQLAAAESRQKKLEMEKLQLQ 146
Cdd:pfam09311 100 MDSREQVSDELVRLQKDNESLQGKHSLHVSLQqaekfdmP-DTVQELQELVLKYREELIEVRTAADHMEEKLKAEILFLK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 147 ALEQEHKKLAAHLEEergknkhVVLMLVKECKqlsgkvvEEAQKLEEVMVKLEEEKKKTSELEDQLSaEKQRS----AGM 222
Cdd:pfam09311 179 EQIQAEQCLKENLEE-------TLQAEIENCK-------EEIASISSLKVELERIKAEKEQLENGLT-EKIRQledlQTT 243
|
170 180 190
....*....|....*....|....*....|....*..
gi 167555091 223 EAQLEKQLFEFDTEREQLRAKLTREEAHTTDLKEEID 259
Cdd:pfam09311 244 KGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELD 280
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-246 |
6.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 132 ESRQKKLEmEKLQLQALEQEHKKLAA---HLEEERgKNKHVVLM-------LVKECKQLSGKVVEEAQKLEEVMVKLEEE 201
Cdd:PRK03918 145 ESREKVVR-QILGLDDYENAYKNLGEvikEIKRRI-ERLEKFIKrtenieeLIKEKEKELEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167555091 202 --------------KKKTSELEDQLSAEKQRSAGMEA---QLEKQLFEFDTEREQLRAKLTR 246
Cdd:PRK03918 223 leklekevkeleelKEEIEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKVKE 284
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
53-228 |
6.88e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 53 EARDLVIEALRARRKEVFIQERYG--RFNLND--PFLALQRDYEAGAGDKEKPVCTNPLSILEAVMAHCRKMQERMSAQL 128
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQqlRMRLSEleQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 129 AAAESRQKKLEMEKlQLQALEQEHKKLAAHLEEERgkNKHVVLMLVKECkqlSGKVVEEAQKLEEVMVKLEEEKKKTSEL 208
Cdd:PRK04863 573 SVSEARERRMALRQ-QLEQLQARIQRLAARAPAWL--AAQDALARLREQ---SGEEFEDSQDVTEYMQQLLERERELTVE 646
|
170 180
....*....|....*....|
gi 167555091 209 EDQLSAEKQRsagMEAQLEK 228
Cdd:PRK04863 647 RDELAARKQA---LDEEIER 663
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
800-825 |
7.00e-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: 35.70 E-value: 7.00e-03
10 20
....*....|....*....|....*.
gi 167555091 800 GQTPLYLACKTGNKECIKLLLEAGTD 825
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGAD 27
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
130-259 |
7.73e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 130 AAESRQKKLEMEKLQ--LQALE--QEHKKLAahLEEERgknkhvvlMLVKECKQLSgKVVEEAQKLEEVMVKLEEEKKKT 205
Cdd:COG1340 101 LAELNKAGGSIDKLRkeIERLEwrQQTEVLS--PEEEK--------ELVEKIKELE-KELEKAKKALEKNEKLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 206 SELEDQLSAEKQR--SAGMEAQ-LEKQLFEFDTEREQLRAKltREEAHTT-----------------------DLKEEID 259
Cdd:COG1340 170 KELRKEAEEIHKKikELAEEAQeLHEEMIELYKEADELRKE--ADELHKEiveaqekadelheeiielqkelrELRKELK 247
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
100-249 |
7.96e-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: 40.60 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 100 KPVCTNPLSILEAVMAHCRKMQERMsAQLAAAESRQKKLEMEKLQLQALEQEHKKLAAHLEEERGKNKHVVLMLVKECKQ 179
Cdd:TIGR02794 28 KPEPGGGAEIIQAVLVDPGAVAQQA-NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 180 lsgkvVEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLTREEA 249
Cdd:TIGR02794 107 -----AEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEA 171
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
344-710 |
8.50e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 344 VGPSALLIRPGIDRQASHSDLGPSPPTALPSSASRIEENGPSAGNAPDLSNSTPSTPSGTAPAAAQTLGAAPQNHSQAPP 423
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 424 VHSLHSPcANTHPGLNPRIQAARFRFQGNANDPDqngnnTQSPPSRDVSPTSRDNLVAKQLARNTVTqalsrfTSPQAGA 503
Cdd:PHA03307 124 ASPPPSP-APDLSEMLRPVGSPGPPPAASPPAAG-----ASPAAVASDAASSRQAALPLSSPEETAR------APSSPPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 504 SSRLGASPGGDAGTCPPVGRtglktPGAARVDRgnpppippkkpglsqtPSPPHPQLRASNAGAKVDnkivaSPPSTLPQ 583
Cdd:PHA03307 192 EPPPSTPPAAASPRPPRRSS-----PISASASS----------------PAPAPGRSAADDAGASSS-----DSSSSESS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 584 GTKVVNEENVPKSSSPQLPPKPSIDLTVASAGCPVSALATSQVGAWPAETP---------GLNQPACTDSSLVIPTTVAF 654
Cdd:PHA03307 246 GCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPspspsspgsGPAPSSPRASSSSSSSRESS 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 167555091 655 RSSINPVSASSRSPGASDSLLVTASGwSPSLTPLLMSGGPAPLAGRPTLLQQAAAQ 710
Cdd:PHA03307 326 SSSTSSSSESSRGAAVSPGPSPSRSP-SPSRPPPPADPSSPRKRPRPSRAPSSPAA 380
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
748-853 |
8.57e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 40.59 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 748 DCVRLLLNAEARVDAADKNGFTPLCVAAAQGHFECIELLT---AYNANINHSAAGGQTPLYLACKTGNK---ECIKLLLE 821
Cdd:PHA02798 90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169
|
90 100 110
....*....|....*....|....*....|....*..
gi 167555091 822 AGTD-RSIKTRDGWTPIHA----AVDTGNVDSLKLLM 853
Cdd:PHA02798 170 KGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFV 206
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
173-259 |
9.14e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167555091 173 LVKECKQLSGkvvEEAQKLEEVMVKLEEEKKKTSELEDQLSAEKQRSAGMEAQLEKQLFEFDTEREQLRAKLtREEAH-- 250
Cdd:PRK00409 503 IIEEAKKLIG---EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA-EKEAQqa 578
|
....*....
gi 167555091 251 TTDLKEEID 259
Cdd:PRK00409 579 IKEAKKEAD 587
|
|
| |
