|
Name |
Accession |
Description |
Interval |
E-value |
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1113-1182 |
2.17e-30 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 114.85 E-value: 2.17e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1113 AKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNT 70
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
856-1177 |
2.37e-17 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 84.19 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 856 MKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREflmlegadpdsieavanrvlelsipasp 935
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE---------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 936 kqIRHLADEIKDRVKSLSNVdaiLEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQaaaekaiekar 1015
Cdd:COG1340 62 --LREKRDELNEKVKELKEE---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1016 ndigltqnrlaQIQSETTAQERDLdnaMDRLGDLGRQIEALKTKR-ANNSLDAARAEetATMARDKANEAKEILdGELSD 1094
Cdd:COG1340 126 -----------QTEVLSPEEEKEL---VEKIKELEKELEKAKKALeKNEKLKELRAE--LKELRKEAEEIHKKI-KELAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KyrtvqglMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAIN 1174
Cdd:COG1340 189 E-------AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKE 261
|
...
gi 2516233906 1175 KKI 1177
Cdd:COG1340 262 KEE 264
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
668-1168 |
4.24e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 668 RAKELQTTGLTRAFE--RKFNDlEGKLAQAREIVNARNAtaEAVTilmgMIEELRGQIGET----TETLNQLEGDLTAVQ 741
Cdd:PTZ00121 1189 KAEELRKAEDARKAEaaRKAEE-ERKAEEARKAEDAKKA--EAVK----KAEEAKKDAEEAkkaeEERNNEEIRKFEEAR 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 742 DSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNFLGAYDSIRTSYNTSRDAENRANKsatdipstvsqsADTRKK 821
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK------------AEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 822 TERLMSEKRDDFNRKNAANKRtltdlNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDaKKKVDHSNNDLRDL 901
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKA-----EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 902 IKQIREFLMLEGADPDSIEAV-----ANRVLELSIPASPKQirhLADEIKDRVKSLSNVDAILEQTQnDVRKAEQLLLDA 976
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkaeeKKKADEAKKKAEEAK---KADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 977 KKARnKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEAL 1056
Cdd:PTZ00121 1480 EEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1057 KTKRANNSLDAARAEETATMARDKANEAKEILDG---ELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKE------L 1127
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkkveqL 1638
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2516233906 1128 LKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDglEDKMKA 1168
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE--EDKKKA 1677
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
237-282 |
1.21e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 71.96 E-value: 1.21e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 237 CECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGFGPSGC 282
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
236-283 |
7.55e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 7.55e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 236 PCECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGF--GPSGCK 283
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
639-1197 |
8.88e-15 |
|
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: 79.72 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 639 PDCKPCHQCFGDWDRIVQDLATRTKALTDRAKELQttGLTRAFERKFNDLEGKLAQAReivnARnataeaVTILMGMIEE 718
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELR--EELEEAEQALDAAERELAQLQ----AR------LDSLERLQEN 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 719 LRG-QIGETTETLNQ--LEGDLTAVQ-----DSNYEAsnALSTLEREAkeLNL----NSDQLNRQLEILKNSN-----FL 781
Cdd:TIGR02168 501 LEGfSEGVKALLKNQsgLSGILGVLSelisvDEGYEA--AIEAALGGR--LQAvvveNLNAAKKAIAFLKQNElgrvtFL 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 782 gAYDSIRTSYNTSRDAENRAN------------KSATDIPSTVS-------------QSADTRKKT---ERLMSEKRDDF 833
Cdd:TIGR02168 577 -PLDSIKGTEIQGNDREILKNiegflgvakdlvKFDPKLRKALSyllggvlvvddldNALELAKKLrpgYRIVTLDGDLV 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 834 NRKNA----ANKRTLTDLNAKAQLldmKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREfl 909
Cdd:TIGR02168 656 RPGGVitggSAKTNSSILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 910 mlegadpdsieavanrvLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDT 989
Cdd:TIGR02168 731 -----------------LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 990 TVSVKQALNDAGKAQaaaekaiekaRNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAAR 1069
Cdd:TIGR02168 794 LKEELKALREALDEL----------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1070 AEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQ 1149
Cdd:TIGR02168 864 LEELIEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1150 -----------QVLEGKAKQLDGLEDKMKAILSAINKKIQiyntsglRLGNDSEMSAQE 1197
Cdd:TIGR02168 943 erlseeysltlEEAEALENKIEDDEEEARRRLKRLENKIK-------ELGPVNLAAIEE 994
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
237-282 |
1.69e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 1.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 237 CECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGFG---PSGC 282
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
285-333 |
2.06e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWGFPNCRLCQC 333
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
549-597 |
9.46e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 9.46e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 549 CGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNPKVLCRAC 597
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
655-998 |
1.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 655 VQDLATRTKALTDRAKELQTTGltRAFERKFNDLEGKLAQAREIVN-----------ARNATAEAVTILMGMIEELRGQI 723
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEqleeriaqlskELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 724 GETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNsnflgayDSIRTSYNTSRDAENRANK 803
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-------RIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 804 SAtdipsTVSQSADTRKKTERLMSEKRDDFNRknAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEK 883
Cdd:TIGR02168 851 SE-----DIESLAAEIEELEELIEELESELEA--LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 884 ASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSieavanrvLELSIPASPKQIRHLADEIKDRVKSLSNV--DAI--- 958
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA--------LENKIEDDEEEARRRLKRLENKIKELGPVnlAAIeey 995
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2516233906 959 ---------LEQTQNDVRKAEQLLLDA-----KKARNKaegVKDTTVSVKQALN 998
Cdd:TIGR02168 996 eelkerydfLTAQKEDLTEAKETLEEAieeidREARER---FKDTFDQVNENFQ 1046
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
597-636 |
3.34e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 3.34e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2516233906 597 CDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSG 636
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
285-328 |
4.96e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 4.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWG--FPNC 328
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
597-641 |
6.46e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 6.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 597 CDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSG-TFPDC 641
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-326 |
1.21e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWGFP 326
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
596-645 |
3.31e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 3.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 596 ACDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSGTFPDCKPCH 645
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
548-590 |
3.57e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 3.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 548 PCGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNP 590
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
549-590 |
5.02e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 5.02e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2516233906 549 CGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNP 590
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
668-1199 |
5.80e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 668 RAKELQTTGLTRAFERKFNDLEGKLAQAREIVNarnataEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVQDSNYEa 747
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 748 snalsTLEREAKELNLNSDQLNRQLEILKNsnFLGAYDSIRTSYNTSRdaENRANKSATDIPSTVSQSADTRKKTERLMS 827
Cdd:pfam12128 341 -----TAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRR--SKIKEQNNRDIAGIKDKLAKIREARDRQLA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 828 EKRDDF--------NRKNAAN-----------------KRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALE 882
Cdd:pfam12128 412 VAEDDLqaleselrEQLEAGKlefneeeyrlksrlgelKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 883 KA-SDAKKKVDHSNNDLRDLIKQIREflmLEGADpdsieavaNRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAileq 961
Cdd:pfam12128 492 SElRQARKRRDQASEALRQASRRLEE---RQSAL--------DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIS---- 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 962 tqndvrkAEQLLldakkaRNKAEGVKDTTvSVKQALNDAGkaqaaaeKAIEKARNDIGLTQNRLAQIQSETTAQERDLDN 1041
Cdd:pfam12128 557 -------PELLH------RTDLDPEVWDG-SVGGELNLYG-------VKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1042 AMDRLGDLGRQIEAlktkrANNSLDAARAEETatMARDKANEAKEILdGELSDKYRTVQglmDNKVKTMQEAKQKA-ERL 1120
Cdd:pfam12128 616 AREKQAAAEEQLVQ-----ANGELEKASREET--FARTALKNARLDL-RRLFDEKQSEK---DKKNKALAERKDSAnERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1121 RDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDG-LEDKMKAILSAINKkiqiyntsgLRLGNDSEMSAQEQQ 1199
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaLDAQLALLKAAIAA---------RRSGAKAELKALETW 755
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
492-551 |
8.15e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 8.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNLASGrgcEPCGC 551
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSD---PPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
331-370 |
1.00e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNP 370
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
440-485 |
1.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 440 CRCSNNIDLSDRgaCDRRTGQCLkCLYNTEGPDCGVCKSGYYGDAS 485
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
331-375 |
1.40e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 1.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNPLISLG 375
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
492-547 |
2.53e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 2.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNLAS-GRGCE 547
Cdd:cd00055 2 CDCNGHGSLSGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
682-925 |
1.02e-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: 55.54 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 682 ERKFNDLEGKLAQAREIVNARNATAEAvtiLMGMIEELRGQIGETTETLNQLEGDLTAvqdsnyeasnalstLEREAKEL 761
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQELAA--------------LEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 762 NLNSDQLNRQLEILKN--SNFLGA-YDSIRTSY-------NTSRDAENRANKSATDIPSTVSQSADTRKKTERLmSEKRD 831
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRAlYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 832 DFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAAlEKASDAKkkvdhsnnDLRDLIKQIREFLML 911
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAE--------ELEALIARLEAEAAA 238
|
250
....*....|....
gi 2516233906 912 EGADPDSIEAVANR 925
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
492-546 |
1.50e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 1.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNlASGRGC 546
Cdd:smart00180 1 CDCDPGGSASGTCDPD--------TGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
439-490 |
3.07e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 3.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2516233906 439 SCRCSNNIDLSDRgaCDRRTGQCLkCLYNTEGPDCGVCKSGYYGDASRRN-CR 490
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGgCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
380-438 |
6.41e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 380 PCPCPEGPSSGrhfaATCYQDNrnqqVVCNCNQGYTGSRCEECASGYYGNPSQPGGrCQ 438
Cdd:cd00055 1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
381-437 |
8.74e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 8.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 381 CPCPEGPSSGrhfaATCYQdnrnQQVVCNCNQGYTGSRCEECASGYYGNPSQPGGRC 437
Cdd:pfam00053 1 CDCNPHGSLS----DTCDP----ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
331-370 |
9.32e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 9.32e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNP 370
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
789-1167 |
2.20e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 789 TSYNTSRDAENRANKSA----TDIPSTVSQSADTRKKTERLmsekrdDFNRKNAANKRT-LTDLNA-----KAQLL---- 854
Cdd:NF033838 47 TVTSSGNESQKEHAKEVeshlEKILSEIQKSLDKRKHTQNV------ALNKKLSDIKTEyLYELNVlkeksEAELTsktk 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 855 ------------DMKKINEKVADAKTKAQEAKNKAQAALEKasdakkkvdhsnnDLRDLIKQIREFLMLEGADPDSieAV 922
Cdd:NF033838 121 keldaafeqfkkDTLEPGKKVAEATKKVEEAEKKAKDQKEE-------------DRRNYPTNTYKTLELEIAESDV--EV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 923 ANRVLELsipaspkqIRHLADEIKDRVKsLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDttVSVKQALNDAGK 1002
Cdd:NF033838 186 KKAELEL--------VKEEAKEPRDEEK-IKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRAD--AKLKEAVEKNVA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1003 AQAAAEKAIEKARNDIGltqnrlaqIQSETTAQERDLDNAMDRLGDlgrqiEALKTKRANNSLDAARAEETATMARDKAN 1082
Cdd:NF033838 255 TSEQDKPKRRAKRGVLG--------EPATPDKKENDAKSSDSSVGE-----ETLPSPSLKPEKKVAEAEKKVEEAKKKAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1083 EAKEildgelSDK-------YRTVQ---GLMDNKVKtmqeaKQKAERLRDEAK-----ELLKDAHDKLQ-------RLEE 1140
Cdd:NF033838 322 DQKE------EDRrnyptntYKTLEleiAESDVKVK-----EAELELVKEEAKeprneEKIKQAKAKVEskkaeatRLEK 390
|
410 420
....*....|....*....|....*..
gi 2516233906 1141 LEKDydenQQVLEGKAKQLDGLEDKMK 1167
Cdd:NF033838 391 IKTD----RKKAEEEAKRKAAEEDKVK 413
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
440-483 |
3.66e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2516233906 440 CRCsnNIDLSDRGACDRRTGQCLkCLYNTEGPDCGVCKSGYYGD 483
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
381-430 |
5.99e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 5.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 381 CPCPegpsSGRHFAATCYQDNrnqqVVCNCNQGYTGSRCEECASGYYGNP 430
Cdd:smart00180 1 CDCD----PGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1023-1168 |
6.04e-05 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 45.81 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1023 NRLAQIQSETTAQERDLDNAMdrlGDLGR------QIEALKTKRANNSLD--AARAEETATMARDKANEAKEILDGELSD 1094
Cdd:cd07596 21 KKLSKQAQRLVKRRRELGSAL---GEFGKaliklaKCEEEVGGELGEALSklGKAAEELSSLSEAQANQELVKLLEPLKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KYRTVQGLMD------NKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKA 1168
Cdd:cd07596 98 YLRYCQAVKEtlddraDALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERLKE 177
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
659-1195 |
1.14e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 659 ATRTKALTDRAKELQTTGLTRAFERKFNDLEGKLAQAREIVNarNATAEAVTILMGMIEE---LRGQIGETTETLN-QLE 734
Cdd:NF041483 555 ARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA--DARAEAERIRREAAEEterLRTEAAERIRTLQaQAE 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 735 GDLTAVQD-SNYEASNALStlEREAKELNLNSDQLNrQLEILKNSNFLGAyDSIRTSYNTSrdAENRANKSATDIPSTVS 813
Cdd:NF041483 633 QEAERLRTeAAADASAARA--EGENVAVRLRSEAAA-EAERLKSEAQESA-DRVRAEAAAA--AERVGTEAAEALAAAQE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQlldmKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDH 893
Cdd:NF041483 707 EAARRRREAEETLGSARAEADQERERAREQSEELLASAR----KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRD 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 894 SNNDLRDLIKQirEFLMLEGAdpdsIEAVANRVlelsipaspkqiRHLADEIKDRVKSlsnvDAILEQTqndvRKAEqll 973
Cdd:NF041483 783 SVAGLQEQAEE--EIAGLRSA----AEHAAERT------------RTEAQEEADRVRS----DAYAERE----RASE--- 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 974 lDAKKARNKAEGVKDTTVS-----VKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDldNAMDRLGD 1048
Cdd:NF041483 834 -DANRLRREAQEETEAAKAlaertVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARE--DANRIRSD 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1049 LGRQIEAL---KTKRANNSLDAARAE------ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAER 1119
Cdd:NF041483 911 AAAQADRLigeATSEAERLTAEARAEaerlrdEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAER 990
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1120 LRDEAKELLKDAHDKLQRL-----EELEKDYDENQQVLEGK----AKQLDGLEDKMKAILSAINKKIQiynTSGLRLGND 1190
Cdd:NF041483 991 IRTEAERVKAEAAAEAERLrtearEEADRTLDEARKDANKRrseaAEQADTLITEAAAEADQLTAKAQ---EEALRTTTE 1067
|
....*
gi 2516233906 1191 SEMSA 1195
Cdd:NF041483 1068 AEAQA 1072
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-1126 |
1.17e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 658 LATRTKALTDRAKElQTTGLTRAFERKFNDLEGKLAQAReivnarnATAEAVtilmgmieelrgqIGETTETlnqlegdl 737
Cdd:NF041483 241 LRSSTAAESDQARR-QAAELSRAAEQRMQEAEEALREAR-------AEAEKV-------------VAEAKEA-------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 738 TAVQDSNYEASNALSTleREAKElnlnsdQLNRQLeilknsnflgaydsirtsyntsrdaeNRANKSATDIPSTVSQS-A 816
Cdd:NF041483 292 AAKQLASAESANEQRT--RTAKE------EIARLV--------------------------GEATKEAEALKAEAEQAlA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 817 DTRKKTERLMSEkrddfnrknAANK-RTLTDLNAKAQLLDMKKINEKVAdakTKAQE-AKNKAQAALEKASDAKKKVDHS 894
Cdd:NF041483 338 DARAEAEKLVAE---------AAEKaRTVAAEDTAAQLAKAARTAEEVL---TKASEdAKATTRAAAEEAERIRREAEAE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 895 NNDLRDLIKQIREflMLEGADPDSIEAVANRVLELSIPA-----SPKQIRHLADEIKDRVKSLSNVDAIlEQTQNDVRKA 969
Cdd:NF041483 406 ADRLRGEAADQAE--QLKGAAKDDTKEYRAKTVELQEEArrlrgEAEQLRAEAVAEGERIRGEARREAV-QQIEEAARTA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 970 EQLLldaKKARNKAEGVKDTTvsvkqalndagkaqaaaekaiekarndigltqnrlaqiqseTTAQERDLDNAMDRLGDL 1049
Cdd:NF041483 483 EELL---TKAKADADELRSTA-----------------------------------------TAESERVRTEAIERATTL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1050 GRQI-EALKTKRANNSLDAARAEETATMARDKANEAKEIL---------------DGELSDKYRTVQGLMDNKVKTMQEA 1113
Cdd:NF041483 519 RRQAeETLERTRAEAERLRAEAEEQAEEVRAAAERAARELreeteraiaarqaeaAEELTRLHTEAEERLTAAEEALADA 598
|
490
....*....|...
gi 2516233906 1114 KQKAERLRDEAKE 1126
Cdd:NF041483 599 RAEAERIRREAAE 611
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
783-1159 |
1.24e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 783 AYDSIRTSYNTS---RDAENRANKSATDIPSTVSqsaDTRKKTERLMSEKRDDFNR------KNAANKRTLTD--LNAKA 851
Cdd:NF041483 64 AYDGADIGYQAEqllRNAQIQADQLRADAERELR---DARAQTQRILQEHAEHQARlqaelhTEAVQRRQQLDqeLAERR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 852 QLLDmKKINEKVADAKTKAQEAKNKAQAALEKA-SDAKKKVDHSNNDLRDLIKQIREFLmleGADPDSIEAVANRVL--- 927
Cdd:NF041483 141 QTVE-SHVNENVAWAEQLRARTESQARRLLDESrAEAEQALAAARAEAERLAEEARQRL---GSEAESARAEAEAILrra 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 928 ----ELSIPASPKQIRHLADEIKD-RVKSLSNVDAILEQTQNDVRKAEQLLLDA----KKARNKAEGVkdttvsVKQALN 998
Cdd:NF041483 217 rkdaERLLNAASTQAQEATDHAEQlRSSTAAESDQARRQAAELSRAAEQRMQEAeealREARAEAEKV------VAEAKE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 999 DAGKaqaaaekaiekarndigltqnRLAQIQSETTAQERDLDNAMDRL-GDLGRQIEALKTKrANNSLDAARAE------ 1071
Cdd:NF041483 291 AAAK---------------------QLASAESANEQRTRTAKEEIARLvGEATKEAEALKAE-AEQALADARAEaeklva 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1072 ETATMARDKANE------------AKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEakellkdAHDKLQRLE 1139
Cdd:NF041483 349 EAAEKARTVAAEdtaaqlakaartAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGE-------AADQAEQLK 421
|
410 420 430
....*....|....*....|....*....|.
gi 2516233906 1140 ELEKD-----------YDENQQVLEGKAKQL 1159
Cdd:NF041483 422 GAAKDdtkeyraktveLQEEARRLRGEAEQL 452
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
670-909 |
3.87e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.56 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 670 KELQTTGLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVqdsnyeasn 749
Cdd:pfam06008 45 LEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFAL--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 750 ALSTLEREAKElnlnsdqLNRQLEILKNSNFlgaydsirtsynTSRDAENRANKsatdipstvsqsadtrKKTERLMSEK 829
Cdd:pfam06008 116 PSSDLSRMLAE-------AQRMLGEIRSRDF------------GTQLQNAEAEL----------------KAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 830 RDDFNRKNAANKRTLTDLNakaQLLDmkKINEKVADAKTKAQEAKNKA----------QAALEKASDAKKKVDHSNNDLR 899
Cdd:pfam06008 161 QTWFQSPQEENKALANALR---DSLA--EYEAKLSDLRELLREAAAKTrdanrlnlanQANLREFQRKKEEVSEQKNQLE 235
|
250
....*....|
gi 2516233906 900 DLIKQIREFL 909
Cdd:pfam06008 236 ETLKTARDSL 245
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1077-1197 |
3.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1077 ARDKANEAKEILDGELSDKYRTVQGLMDNKVktmQEAKQKAERLRDEAKELLKDAHDKLQRLEEL----EKDYDENQQVL 1152
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFEKELRERRNELQKLEKRllqkEENLDRKLELL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2516233906 1153 EGKAKQLDGLEDKMKAILSAINKKIQ----IYNTSGLRLGNDSEMSAQE 1197
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEeleeLIEEQLQELERISGLTAEE 154
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1070-1175 |
6.51e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1070 AEETATMARDKA------NEAKEILDgELSDKYRTVQ---GLMDNKVKTMQEAKQK-AERLRDEAKELLKDAHDKLQRLE 1139
Cdd:smart00787 150 DENLEGLKEDYKllmkelELLNSIKP-KLRDRKDALEeelRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110
....*....|....*....|....*....|....*.
gi 2516233906 1140 ELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINK 1175
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
655-910 |
1.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 655 VQDLATRTKALTDRAKELQTTGLTraFERKFNDLEGKLA-QAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQL 733
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQT--LDMKIDHIQQQIKtYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 EGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSnflgayDSIRTSYNTSRDAENRANKSATDIPSTVS 813
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG------GVCPTCTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLmSEKRDDFNRknaaNKRTLTDLNAkaqlldmkKINEKVADAKTKAQEAKnKAQAALEKASDA----KK 889
Cdd:PHA02562 314 SLEKLDTAIDEL-EEIMDEFNE----QSKKLLELKN--------KISTNKQSLITLVDKAK-KVKAAIEELQAEfvdnAE 379
|
250 260
....*....|....*....|.
gi 2516233906 890 KVDHSNNDLRDLIKQIREFLM 910
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSELVK 400
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1082-1183 |
1.57e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1082 NEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKA----ERLRDEAKELLKDAHDKLQRLEELEkdydENQQVLEGKAK 1157
Cdd:pfam10168 538 SRATQVFREEYLKKHDLAREEIQKRVKLLKLQKEQQlqelQSLEEERKSLSERAEKLAEKYEEIK----DKQEKLMRRCK 613
|
90 100 110
....*....|....*....|....*....|....*..
gi 2516233906 1158 QLDGL-----------EDKMKAILSAINKKIQIYNTS 1183
Cdd:pfam10168 614 KVLQRlnsqlpvlsdaEREMKKELETINEQLKHLANA 650
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1113-1182 |
2.17e-30 |
|
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called laminin B1s chain, laminin-11 subunit beta, laminin-14 subunit beta, laminin-15 subunit beta, laminin-3 subunit beta, laminin-4 subunit beta, laminin-7 subunit beta, laminin-9 subunit beta, S-laminin subunit beta, or S-LAM beta (LAMS). It is an important component of the interphotoreceptor matrix and plays a role in rod morphogenesis. It may also have an important function in the sarcolemmal basement membrane. Mutations of the LAMB2 gene mainly cause Pierson syndrome (microcoria-congenital nephrosis syndrome). LAMB2 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB2, which may be involved in the integrin binding activity.
Pssm-ID: 411970 [Multi-domain] Cd Length: 72 Bit Score: 114.85 E-value: 2.17e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1113 AKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNT 70
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1112-1182 |
7.98e-22 |
|
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called laminin B1 chain, laminin-1 subunit beta, laminin-10 subunit beta, laminin-12 subunit beta, laminin-2 subunit beta, laminin-6 subunit beta, or laminin-8 subunit beta. It is a glycoprotein that is involved in the pathogenesis of neurodevelopmental disorders. It also plays a crucial role in both lung morphogenesis and physiological function. Mutations in LAMB1 are associated with Cobblestone brain malformation (COB) with variable muscular or ocular abnormalities. LAMB1 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB1, which is involved in the integrin binding activity.
Pssm-ID: 411971 [Multi-domain] Cd Length: 73 Bit Score: 90.23 E-value: 7.98e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 1112 EAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYST 71
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1115-1182 |
5.43e-18 |
|
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family contains four members, LAMB1-4. They are components of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB, which may be involved in the integrin binding activity.
Pssm-ID: 411969 [Multi-domain] Cd Length: 70 Bit Score: 79.25 E-value: 5.43e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1115 QKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22295 2 DRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYAT 69
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
856-1177 |
2.37e-17 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 84.19 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 856 MKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREflmlegadpdsieavanrvlelsipasp 935
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQE---------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 936 kqIRHLADEIKDRVKSLSNVdaiLEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQaaaekaiekar 1015
Cdd:COG1340 62 --LREKRDELNEKVKELKEE---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ----------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1016 ndigltqnrlaQIQSETTAQERDLdnaMDRLGDLGRQIEALKTKR-ANNSLDAARAEetATMARDKANEAKEILdGELSD 1094
Cdd:COG1340 126 -----------QTEVLSPEEEKEL---VEKIKELEKELEKAKKALeKNEKLKELRAE--LKELRKEAEEIHKKI-KELAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KyrtvqglMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAIN 1174
Cdd:COG1340 189 E-------AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKE 261
|
...
gi 2516233906 1175 KKI 1177
Cdd:COG1340 262 KEE 264
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
668-1168 |
4.24e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 668 RAKELQTTGLTRAFE--RKFNDlEGKLAQAREIVNARNAtaEAVTilmgMIEELRGQIGET----TETLNQLEGDLTAVQ 741
Cdd:PTZ00121 1189 KAEELRKAEDARKAEaaRKAEE-ERKAEEARKAEDAKKA--EAVK----KAEEAKKDAEEAkkaeEERNNEEIRKFEEAR 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 742 DSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNFLGAYDSIRTSYNTSRDAENRANKsatdipstvsqsADTRKK 821
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK------------AEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 822 TERLMSEKRDDFNRKNAANKRtltdlNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDaKKKVDHSNNDLRDL 901
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKA-----EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEED 1403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 902 IKQIREFLMLEGADPDSIEAV-----ANRVLELSIPASPKQirhLADEIKDRVKSLSNVDAILEQTQnDVRKAEQLLLDA 976
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKkkaeeKKKADEAKKKAEEAK---KADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 977 KKARnKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEAL 1056
Cdd:PTZ00121 1480 EEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1057 KTKRANNSLDAARAEETATMARDKANEAKEILDG---ELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKE------L 1127
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkkveqL 1638
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2516233906 1128 LKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDglEDKMKA 1168
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE--EDKKKA 1677
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
237-282 |
1.21e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 71.96 E-value: 1.21e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 237 CECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGFGPSGC 282
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
679-1168 |
2.07e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 679 RAFERKFNDLEGKLAQAREIVNARNAT----AEAV--TILMGMIEELR-GQIGETTETLNQLEGDLTAVQDSNYEASNAL 751
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEdakkAEAArkAEEVRKAEELRkAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 752 STLEReAKELNLNSDQLnRQLEILKNSNFLGAYDSIRTSYNTSRDAENRANKSatdipstvsQSADTRKKTErlmsEKRD 831
Cdd:PTZ00121 1227 EAVKK-AEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA---------RKADELKKAE----EKKK 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 832 DFNRKNAANKRTLTDLNAKAQllDMKKINEkvadAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLML 911
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAE--EAKKADE----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 912 EGADPDSIEAVANRVLELSIPASPK----QIRHLADEIKDRVKSLSNVDAI------LEQTQNDVRKAEQLLLDAKKARn 981
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAkkkadeAKKKAEEKKKADEAKKKAEEAK- 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 982 KAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDiglTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRA 1061
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1062 NNSLDAARAEEtatmaRDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEA---KELLKDAHDKlqRL 1138
Cdd:PTZ00121 1522 KKADEAKKAEE-----AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkAEEAKKAEEA--RI 1594
|
490 500 510
....*....|....*....|....*....|
gi 2516233906 1139 EELEKDYDENQQVLEGKAKQLDglEDKMKA 1168
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAE--EAKIKA 1622
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
236-283 |
7.55e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 7.55e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 236 PCECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGF--GPSGCK 283
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
639-1197 |
8.88e-15 |
|
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: 79.72 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 639 PDCKPCHQCFGDWDRIVQDLATRTKALTDRAKELQttGLTRAFERKFNDLEGKLAQAReivnARnataeaVTILMGMIEE 718
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELR--EELEEAEQALDAAERELAQLQ----AR------LDSLERLQEN 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 719 LRG-QIGETTETLNQ--LEGDLTAVQ-----DSNYEAsnALSTLEREAkeLNL----NSDQLNRQLEILKNSN-----FL 781
Cdd:TIGR02168 501 LEGfSEGVKALLKNQsgLSGILGVLSelisvDEGYEA--AIEAALGGR--LQAvvveNLNAAKKAIAFLKQNElgrvtFL 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 782 gAYDSIRTSYNTSRDAENRAN------------KSATDIPSTVS-------------QSADTRKKT---ERLMSEKRDDF 833
Cdd:TIGR02168 577 -PLDSIKGTEIQGNDREILKNiegflgvakdlvKFDPKLRKALSyllggvlvvddldNALELAKKLrpgYRIVTLDGDLV 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 834 NRKNA----ANKRTLTDLNAKAQLldmKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREfl 909
Cdd:TIGR02168 656 RPGGVitggSAKTNSSILERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 910 mlegadpdsieavanrvLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDT 989
Cdd:TIGR02168 731 -----------------LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 990 TVSVKQALNDAGKAQaaaekaiekaRNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAAR 1069
Cdd:TIGR02168 794 LKEELKALREALDEL----------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1070 AEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQ 1149
Cdd:TIGR02168 864 LEELIEELESELEALLNERA-SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1150 -----------QVLEGKAKQLDGLEDKMKAILSAINKKIQiyntsglRLGNDSEMSAQE 1197
Cdd:TIGR02168 943 erlseeysltlEEAEALENKIEDDEEEARRRLKRLENKIK-------ELGPVNLAAIEE 994
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
684-1178 |
1.77e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 684 KFNDLEGKLAQAREIV--------NARNATAEAVTIL------MGMIEELRGQIGETTETLNQLEGDLTAVQDSNYEASN 749
Cdd:PRK02224 207 RLNGLESELAELDEEIeryeeqreQARETRDEADEVLeeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 750 ALSTLEREAKELNLNSDqlnrqLEilknsnflgaydsirtsyntsrDAENRAnksatdipstvsqsadtrkkterlMSEK 829
Cdd:PRK02224 287 RLEELEEERDDLLAEAG-----LD----------------------DADAEA------------------------VEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 830 RDDFNRKNAANKRTLTD--LNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIRE 907
Cdd:PRK02224 316 REELEDRDEELRDRLEEcrVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 908 FLMLEGADPDSIEAVANRVLELsipaspkqiRHLADEIKDRVKSLSnvdAILEQTQNDVRKAEQlLLDAKKARNKAEGVK 987
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEEL---------REERDELREREAELE---ATLRTARERVEEAEA-LLEAGKCPECGQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 988 DTtvSVKQALNDAgkaqaaaekaiekaRNDIGLTQNRLAQIQSETTAQERDLDNAMDrLGDLGRQIEALKTKRANNSLDA 1067
Cdd:PRK02224 463 GS--PHVETIEED--------------RERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1068 ARAEETATMARDKA---NEAKEILDGElsdkyrtvqglMDNKVKTMQEAKQKAERLRDEAKEL------LKDAHDKLQRL 1138
Cdd:PRK02224 526 AERRETIEEKRERAeelRERAAELEAE-----------AEEKREAAAEAEEEAEEAREEVAELnsklaeLKERIESLERI 594
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2516233906 1139 EELEKDYDENQQVLEG---KAKQLDGLEDKMKAILSAINKKIQ 1178
Cdd:PRK02224 595 RTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKR 637
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-1172 |
6.06e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 6.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 659 ATRTKALTDRAKELQTtgltRAFERKFNDLEGKLAQAREIVNARNATAEAvtiLMGMIEELRGQIGETTETLNQLEGDLT 738
Cdd:COG1196 212 AERYRELKEELKELEA----ELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 739 AVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKnsnflgaydsirtsyntsrDAENRANKSATDIPSTVSQSADT 818
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-------------------EELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 819 RKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQLLDmkKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDL 898
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE--ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 899 RDLIKQIREFLMLEGADPDSIEAVANRVLELSipaspKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKK 978
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELE-----EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 979 ARNKAEGVKDTTVSVKQALNDAGKAQAAaekaiekarnDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKT 1058
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAV----------AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1059 KRA-------NNSLDAARAEETAT--MARDKANEAKEILDGELSDKYRTVQGLM---DNKVKTMQEAKQKAERLRDEAKE 1126
Cdd:COG1196 569 AKAgratflpLDKIRARAALAAALarGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2516233906 1127 LLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSA 1172
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
659-1178 |
1.10e-13 |
|
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: 76.25 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 659 ATRTKALTDRAKELQTTGLTRaferKFNDLEGKLAQAREIVNA----RNATAEAVTILMGMIEELRGQIGETTETLNQLE 734
Cdd:TIGR02168 212 AERYKELKAELRELELALLVL----RLEELREELEELQEELKEaeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 735 GDLtavqdsnYEASNALSTLEREAKELNLNSDQLNRQLEILKnsnflgayDSIRTSYNTSRDAENRANKSATDIPSTVSQ 814
Cdd:TIGR02168 288 KEL-------YALANEISRLEQQKQILRERLANLERQLEELE--------AQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 815 SADTRKKTERLmSEKRDDFNRKNAANKRTLTDLNAK-AQL-LDMKKINEKVADAKTKAQE-AKNKAQAALEKASDAKKKV 891
Cdd:TIGR02168 353 LESLEAELEEL-EAELEELESRLEELEEQLETLRSKvAQLeLQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 892 DHSNNDLRDLIKQIREflMLEGAdpdsIEAVANRVLEL-SIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAE 970
Cdd:TIGR02168 432 EAELKELQAELEELEE--ELEEL----QEELERLEEALeELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 971 QLLLDAKKARNKAEGVKDTT---VSVK---------------QAL-----NDAGKAQAAAEKAIEKARNDIGLTQNRLAQ 1027
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLselISVDegyeaaieaalggrlQAVvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1028 IQSETTAQERDLDNAMDRLGDLGRQIEALKtKRANNSLDAARAEETATMARDKANEAKE-----ILDGELSDKYRTVQGL 1102
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLR-KALSYLLGGVLVVDDLDNALELAKKLRPgyrivTLDGDLVRPGGVITGG 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1103 MDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDK---MKAILSAINKKIQ 1178
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVE 743
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
237-282 |
1.69e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 65.84 E-value: 1.69e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 237 CECDSQGSLSSECDVRGGQCRCKPNVSGRRCDKCAPGAYGFG---PSGC 282
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPsdpPQGC 49
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
756-1168 |
7.32e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 756 REAKELNLNSDQLNRQLEILKNSnflgAYDSIRTSYNTSRDAENRANKSATdipSTVSQSADTRKKTErlmSEKRDDFNR 835
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEA---AEEKAEAAEKKKEE---AKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 836 KNAANKRTLTDLNAKAQLlDMKKINE--KVADAKTKAQEAKNKAQAaLEKASDAKKKVDHSNNdLRDLIKQIREFLMLEG 913
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEE-DKKKADElkKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 914 ADPDSIEAvaNRVLELSIPASPKQirhLADEIKDRVKSLSNVDAILEQTQNDVRKAEQllldAKKARNKAEGVKDTTVSV 993
Cdd:PTZ00121 1462 AKKKAEEA--KKADEAKKKAEEAK---KADEAKKKAEEAKKKADEAKKAAEAKKKADE----AKKAEEAKKADEAKKAEE 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 994 KQALNDAGKAQAAAEKAIEKARNDIGLTQNRlAQIQSETTAQERDldNAMDRLGDLGRQIEalktKRANNSLDAARAEET 1073
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEK-KKAEEAKKAEEDK--NMALRKAEEAKKAE----EARIEEVMKLYEEEK 1605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1074 ATMARDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDE-------AKELLKDAHDKLQRLEELEKDYD 1146
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkikAAEEAKKAEEDKKKAEEAKKAEE 1685
|
410 420
....*....|....*....|..
gi 2516233906 1147 ENQQVLEGKAKQldgLEDKMKA 1168
Cdd:PTZ00121 1686 DEKKAAEALKKE---AEEAKKA 1704
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1114-1182 |
9.00e-13 |
|
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) and similar proteins; DmLAMB1, also called LanB1, is a glycoprotein required for nidogen (Ndg) localization to the basement membrane. It is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of DmLAMB1, which may be involved in the integrin binding activity.
Pssm-ID: 411973 [Multi-domain] Cd Length: 70 Bit Score: 64.56 E-value: 9.00e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1114 KQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRT 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
652-1175 |
9.33e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 652 DRIVQDLATRTKALTDRAKELQTtgLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLN 731
Cdd:COG1196 249 EELEAELEELEAELAELEAELEE--LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 732 QLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEiLKNSNFLGAYDSIRTSYNTSRDAENRANKSATDIPST 811
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 812 VSQSADTRKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQLLdmkkinEKVADAKTKAQEAKNKAQAALEKASDAKKKV 891
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA------EEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 892 DHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRVLelsIPASPKQIRHLADEIKDRVK--------SLSNVDAILEQTQ 963
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL---LAGLRGLAGAVAVLIGVEAAyeaaleaaLAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 964 NDVRKAEQLLLDAKKAR------NKAEGVKDTTVSVKQALNDAG-----------KAQAAAEKAIEKARNDIGLTQNRLA 1026
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRatflplDKIRARAALAAALARGAIGAAvdlvasdlreaDARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1027 QIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSL----------DAARAEETATMARDKANEAKEILDGELSDKY 1096
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLeaeaeleelaERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1097 RTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDA----------HDKLQ-RLEELEK--------------DYDENQQV 1151
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdLEELErELERLEReiealgpvnllaieEYEELEER 796
|
570 580
....*....|....*....|....
gi 2516233906 1152 LEGKAKQLDGLEDKMKAILSAINK 1175
Cdd:COG1196 797 YDFLSEQREDLEEARETLEEAIEE 820
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
285-333 |
2.06e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 2.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWGFPNCRLCQC 333
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
656-1175 |
4.04e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 656 QDLATRTKALTDRAKELQT--TGLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQL 733
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 EGDLTAVQDSNYEASNALSTLEReaKELNLNSDQLNRQLEILKnsnflGAYDSIRTSYNTSRDAENRANKSATDIPSTVS 813
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQ-----EELERLEEALEELREELEEAEQALDAAERELA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLMSEKRDDFN--RKNAANKRTLTDLnaKAQLLDMKKINEKVADAKTKA------------QEAKNKAQA 879
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEgvKALLKNQSGLSGI--LGVLSELISVDEGYEAAIEAAlggrlqavvvenLNAAKKAIA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 880 ALEKASDAK--------KKVDHSNNDLRDLIKQIREFLMLeGADPDSIEAVANRVLE-----LSIPASPKQIRHLADEIK 946
Cdd:TIGR02168 564 FLKQNELGRvtflpldsIKGTEIQGNDREILKNIEGFLGV-AKDLVKFDPKLRKALSyllggVLVVDDLDNALELAKKLR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 947 ----------DRV--------KSLSNVDAILEQTQN------DVRKAEQLLLDAKKARNKAEgvkdttvsvkQALNDAGK 1002
Cdd:TIGR02168 643 pgyrivtldgDLVrpggvitgGSAKTNSSILERRREieeleeKIEELEEKIAELEKALAELR----------KELEELEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1003 AQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEET-----ATMA 1077
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeleAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1078 RDK--ANEAKEILDgELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGK 1155
Cdd:TIGR02168 793 QLKeeLKALREALD-ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
570 580
....*....|....*....|
gi 2516233906 1156 AKQLDGLEDKMKAILSAINK 1175
Cdd:TIGR02168 872 ESELEALLNERASLEEALAL 891
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
690-1173 |
5.39e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 690 GKLAQAREIV-NARNATAEAVTILMGMIEELRGQIGETTET-----LNQLEGDLTAVQDS--NYEASNALSTLEREAKEL 761
Cdd:PRK02224 162 GKLEEYRERAsDARLGVERVLSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEieRYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 762 NLNSDQLNRQ-LEILK------NSNFLGAYDSIRTSYNTSRDAENRANKSATDIPSTVSQSADTRKKTERLmSEKRDDFN 834
Cdd:PRK02224 242 VLEEHEERREeLETLEaeiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV-EARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 835 RKNAANKRTLTD--LNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLE 912
Cdd:PRK02224 321 DRDEELRDRLEEcrVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 913 GADPDSIEAVANRVLELsipaspkqiRHLADEIKDRVKSLSnvdAILEQTQNDVRKAEQLLlDAKKARNKAEGVKDTtvS 992
Cdd:PRK02224 401 GDAPVDLGNAEDFLEEL---------REERDELREREAELE---ATLRTARERVEEAEALL-EAGKCPECGQPVEGS--P 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 993 VKQALNDAgkaqaaaekaiekaRNDIGLTQNRLAQIQSETTAQERDLDNAMDrLGDLGRQIEALKTKRannsldaaraee 1072
Cdd:PRK02224 466 HVETIEED--------------RERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERR------------ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1073 tatmardkaneakeildgelsdkyRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQV- 1151
Cdd:PRK02224 519 ------------------------EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEv 574
|
490 500
....*....|....*....|....*...
gi 2516233906 1152 --LEGK----AKQLDGLEdKMKAILSAI 1173
Cdd:PRK02224 575 aeLNSKlaelKERIESLE-RIRTLLAAI 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
716-1137 |
9.33e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 716 IEELRGQIGETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNFLGAYDSIRTSYNTSr 795
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT- 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 796 DAENRANKSATDIPSTVSQSADTRKKTERLmSEKRDDFNRKNAANKRTLTDLNAKAQLLdmkkinekvadaKTKAQEAKN 875
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEEL-EAQIEQLKEELKALREALDELRAELTLL------------NEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 876 KAQAALEKASDAKKkvdhSNNDLRDLIKQIREflmlegadpdSIEAVANRV--LELSIPASPKQIRHLADEIKDRVKSLS 953
Cdd:TIGR02168 825 RLESLERRIAATER----RLEDLEEQIEELSE----------DIESLAAEIeeLEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 954 NVDAILEQTQNDVRKAEQlllDAKKARNKAEGVKDTTVSVKQALNdagKAQAAAEKAIEKARNDIGLTQNRLAQIQSETT 1033
Cdd:TIGR02168 891 LLRSELEELSEELRELES---KRSELRRELEELREKLAQLELRLE---GLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1034 AQERDLDnamDRLGDLGRQIEALKtkRAN-NSLDAARAEetatmardkaNEAKEILDGELSDKYRTVQGLMdnkvKTMQE 1112
Cdd:TIGR02168 965 DDEEEAR---RRLKRLENKIKELG--PVNlAAIEEYEEL----------KERYDFLTAQKEDLTEAKETLE----EAIEE 1025
|
410 420
....*....|....*....|....*
gi 2516233906 1113 akqkaerLRDEAKELLKDAHDKLQR 1137
Cdd:TIGR02168 1026 -------IDREARERFKDTFDQVNE 1043
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
549-597 |
9.46e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 9.46e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2516233906 549 CGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNPKVLCRAC 597
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
655-998 |
1.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 655 VQDLATRTKALTDRAKELQTTGltRAFERKFNDLEGKLAQAREIVN-----------ARNATAEAVTILMGMIEELRGQI 723
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEqleeriaqlskELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 724 GETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNsnflgayDSIRTSYNTSRDAENRANK 803
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-------RIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 804 SAtdipsTVSQSADTRKKTERLMSEKRDDFNRknAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEK 883
Cdd:TIGR02168 851 SE-----DIESLAAEIEELEELIEELESELEA--LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 884 ASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSieavanrvLELSIPASPKQIRHLADEIKDRVKSLSNV--DAI--- 958
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEA--------LENKIEDDEEEARRRLKRLENKIKELGPVnlAAIeey 995
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2516233906 959 ---------LEQTQNDVRKAEQLLLDA-----KKARNKaegVKDTTVSVKQALN 998
Cdd:TIGR02168 996 eelkerydfLTAQKEDLTEAKETLEEAieeidREARER---FKDTFDQVNENFQ 1046
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
746-1206 |
2.78e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 746 EASNALSTLEREAKELNlNSDQLNRQLEILKNSNflgayDSIRTSYNTSRDAEnRANKSATDipstVSQSADTRKKTERl 825
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKA-----DELKKAAAAKKKAD-EAKKKAEE----KKKADEAKKKAEE- 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 826 msEKRDDFNRKNAANKRTLTDLNAKAQllDMKKINE--KVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNdlRDLIK 903
Cdd:PTZ00121 1443 --AKKADEAKKKAEEAKKAEEAKKKAE--EAKKADEakKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 904 QIREflmLEGADPDSIEAVANRVLELSIPASPKQIRHL--ADEIK--DRVKSLSNVDAILEQTQNDVRKAEQL------- 972
Cdd:PTZ00121 1517 KAEE---AKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAkkaeear 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 973 ------------------LLDAKKARNKAEGVKDTTvSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTA 1034
Cdd:PTZ00121 1594 ieevmklyeeekkmkaeeAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1035 QERDLDNAMDRLGDLGRQIEALKTKRAnnslDAARAEETATMARDKANEAKEILDGELSDKYRTVQGlmdnkVKTMQEAK 1114
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAE----EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA-----KKEAEEDK 1743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1115 QKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLD-----GLEDKMKAILSAINKKIQIYNTSGLRLGN 1189
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDekrrmEVDKKIKDIFDNFANIIEGGKEGNLVIND 1823
|
490
....*....|....*..
gi 2516233906 1190 DSEMSAQEQQPSTLTSN 1206
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKN 1840
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
597-636 |
3.34e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 59.29 E-value: 3.34e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2516233906 597 CDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSG 636
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
285-328 |
4.96e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.86 E-value: 4.96e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWG--FPNC 328
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
921-1178 |
6.34e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 921 AVANRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRK--AEQLLLDAKKARNKAEGVKDTtvsvkQALN 998
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEleAELAELEAELEELRLELEELE-----LELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 999 DAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDLDNamdrlgdLGRQIEALKTKRANNSLDAARAEETATMAR 1078
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE-------LEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1079 DKANEAKEILDgELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQ 1158
Cdd:COG1196 358 AELAEAEEALL-EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260
....*....|....*....|
gi 2516233906 1159 LDGLEDKMKAILSAINKKIQ 1178
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEE 456
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
597-641 |
6.46e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 6.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 597 CDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSG-TFPDC 641
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
650-1182 |
8.01e-11 |
|
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: 66.58 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 650 DWDRIVQDLATRTKALTDRAKELqttgltrafERKFNDLEGKLAQAREIVNARNATaeavtiLMGMIEEL---RGQIGET 726
Cdd:TIGR04523 58 NLDKNLNKDEEKINNSNNKIKIL---------EQQIKDLNDKLKKNKDKINKLNSD------LSKINSEIkndKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 727 TETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNS--NFLGAYDSIRTSYNTSRDAENRANKS 804
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 805 ATDIpstvsqsaDTRKKTERLMSEKRDDFNRKNAANKRTLTDLNakaqlldmKKINEKVA---DAKTKAQEAKNKAQAAL 881
Cdd:TIGR04523 203 LSNL--------KKKIQKNKSLESQISELKKQNNQLKDNIEKKQ--------QEINEKTTeisNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 882 EKASDAKKKVDHSNNDLRDLIKQIREflmlegadpdsIEAvanrvlELSIPASPKQirhlADEIKDrVKS-LSNVDAILE 960
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQ-----------LKS------EISDLNNQKE----QDWNKE-LKSeLKNQEKKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 961 QTQNDVRKAEQLLLDakkarnkaegVKDTTVSVKQALNDagkaqaaaekaiekARNDIGLTQNRLAQIQSETTAQERDLD 1040
Cdd:TIGR04523 325 EIQNQISQNNKIISQ----------LNEQISQLKKELTN--------------SESENSEKQRELEEKQNEIEKLKKENQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1041 NAMDRLGDLGRQIEALKTKRANNsldaaraeetatmarDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERL 1120
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQ---------------EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1121 RDE--AKELLKDAHDKL-----QRLEELEKDYDENQQVLEGKAKQLDgleDKMKAILSAINKKIQIYNT 1182
Cdd:TIGR04523 446 TNQdsVKELIIKNLDNTresleTQLKVLSRSINKIKQNLEQKQKELK---SKEKELKKLNEEKKELEEK 511
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
285-326 |
1.21e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 1.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2516233906 285 CECSLEGSQSRFCDQRTGQCPCQPGAFGQRCDGCQGGHWGFP 326
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
695-1201 |
1.68e-10 |
|
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: 65.36 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 695 AREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEGDLTaVQDSNyeasnalSTLEREAKELNLNSDQLNRQLEI 774
Cdd:COG5185 157 ETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEP-SGTVN-------SIKESETGNLGSESTLLEKAKEI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 775 LKNSNFLgaydsirtsyntsrdaenranKSATDIPSTVSQSADTRKKTERLMsEKRDDFNRKNAANKRTLtdlnakaqll 854
Cdd:COG5185 229 INIEEAL---------------------KGFQDPESELEDLAQTSDKLEKLV-EQNTDLRLEKLGENAES---------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 855 dMKKINEKVADAKTKAQEAKNKAQAALEKASDAKkkvdhsnnDLRDLIKQIREFlmlegadpdsiEAVANrvLELSIPAS 934
Cdd:COG5185 277 -SKRLNENANNLIKQFENTKEKIAEYTKSIDIKK--------ATESLEEQLAAA-----------EAEQE--LEESKRET 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 935 PKQIRHLADEIKDRVKSL-SNVDAILEQTQNDVRKAEQLLLDAkkarnKAEGVKDTTVSVKQALNDAGKAQAaaekaiek 1013
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLtENLEAIKEEIENIVGEVELSKSSE-----ELDSFKDTIESTKESLDEIPQNQR-------- 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1014 arndiGLTQNRLAQIQSETTAQERDLDNamdrlgdLGRQIEALKTKRAnnsldaaraeetatmardkanEAKEILDGELS 1093
Cdd:COG5185 402 -----GYAQEILATLEDTLKAADRQIEE-------LQRQIEQATSSNE---------------------EVSKLLNELIS 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1094 DKYRTVQGLMDNKVKTMQEAKQKAERlrdEAKELLKDAHDKLQRLEelekdydenQQVLEGKAKqLDGLEDKMKAILSAI 1173
Cdd:COG5185 449 ELNKVMREADEESQSRLEEAYDEINR---SVRSKKEDLNEELTQIE---------SRVSTLKAT-LEKLRAKLERQLEGV 515
|
490 500 510
....*....|....*....|....*....|..
gi 2516233906 1174 NKKIQIY----NTSGLRLGNDSEMSAQEQQPS 1201
Cdd:COG5185 516 RSKLDQVaeslKDFMRARGYAHILALENLIPA 547
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1017-1213 |
2.47e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1017 DIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTK--RANNSLDAARAEETAtmARDKANEAKEILDGELSD 1094
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEleALQAEIDKLQAEIAE--AEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KYR----------------------------TVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYD 1146
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 1147 ENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNTSGLRLGNDSEMSAQEQQPSTLTSNAAKIAGP 1213
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
813-1148 |
3.02e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 813 SQSADTRKKTERLmSEKRDDFNRKNAANKRTLTDLNAKAQLLDMK--KINEKVADAKTKAQEAKNKAQAALEKASDAKKK 890
Cdd:COG1340 1 SKTDELSSSLEEL-EEKIEELREEIEELKEKRDELNEELKELAEKrdELNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 891 VDHSNNDLRDLIKQIREF------LMLEGADPDSIEavanrvlelsipaspKQIRHLADEIKDRVKSLSNVDAILEQtqn 964
Cdd:COG1340 80 RDELNEKLNELREELDELrkelaeLNKAGGSIDKLR---------------KEIERLEWRQQTEVLSPEEEKELVEK--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 965 dVRKAEQLLLDAKKARNKAEGVKDT---TVSVKQALNDAGKaqaaaekaiekarndigltqnrlaQIQseTTAQERDldN 1041
Cdd:COG1340 142 -IKELEKELEKAKKALEKNEKLKELraeLKELRKEAEEIHK------------------------KIK--ELAEEAQ--E 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1042 AMDRLGDLGRQIEALKTKRannslDAARAEetATMARDKANEAKEILDgELSDKYRTVQGLMDnKVKTMQEAKQKAERlR 1121
Cdd:COG1340 193 LHEEMIELYKEADELRKEA-----DELHKE--IVEAQEKADELHEEII-ELQKELRELRKELK-KLRKKQRALKREKE-K 262
|
330 340 350
....*....|....*....|....*....|..
gi 2516233906 1122 DEAKELLKDAHDKLQR-----LEELEKDYDEN 1148
Cdd:COG1340 263 EELEEKAEEIFEKLKKgekltTEELKLLQKSG 294
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
596-645 |
3.31e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 3.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 596 ACDCDPRGIETSQCDRVSGHCGCRQGVSGVRCDQCARGFSGTFPDCKPCH 645
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
548-590 |
3.57e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 3.57e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 548 PCGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNP 590
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1115-1182 |
4.77e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called laminin beta-1-related protein, is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Mutations or loss of LAMB4 may be features of gastric and colorectal cancers. Reduced LAMB4 levels may contribute to colonic dysmotility associated with diverticulitis. This model corresponds to the C-terminal coiled-coil domain of LAMB4, which may be involved in the integrin binding activity.
Pssm-ID: 411972 [Multi-domain] Cd Length: 70 Bit Score: 56.60 E-value: 4.77e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1115 QKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22301 2 ERLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYST 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
656-1175 |
5.36e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 656 QDLATRTKALTDRAKELQTTgLTRAfERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEG 735
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKE-LEEV-LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 736 DLTAVQDSNYEASNALSTLEREAKELNlnsdqlnrqlEILKNSNflgAYDSIRTSYNTSRDAENRANKSATDIPSTvsqs 815
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELK----------ELKEKAE---EYIKLSEFYEEYLDELREIEKRLSRLEEE---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 816 adtRKKTERLMSEKRDDFNRKNAANK------RTLTDLNAKAQLLDM--KKINEKVADAKTKAQEAKNKAQAALEKASDA 887
Cdd:PRK03918 323 ---INGIEERIKELEEKEERLEELKKklkeleKRLEELEERHELYEEakAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 888 KKKVDHSNNDLRDLI---KQIREFLM-----LEGADpdSIEAVANRvlELSIPASPKQIRHLADEIKDRVKSLSNVDAIL 959
Cdd:PRK03918 400 KEEIEEEISKITARIgelKKEIKELKkaieeLKKAK--GKCPVCGR--ELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 960 EQTQNDVRKAEQLLLDAKKARnKAEGVKDTTVSVKQALN--DAGKAQAAAEKAIEKARNDIGLTQ---------NRLAQI 1028
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELI-KLKELAEQLKELEEKLKkyNLEELEKKAEEYEKLKEKLIKLKGeikslkkelEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1029 QSETTAQERDLDNAMDRLGDLGRQIEALKTKrannSLDaaraeetatmardkanEAKEILdGELSDKYRTVQGLMDNKvK 1108
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFE----SVE----------------ELEERL-KELEPFYNEYLELKDAE-K 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1109 TMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQV-------------------LEGKAKQLDGLEDKMKAI 1169
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
....*.
gi 2516233906 1170 LSAINK 1175
Cdd:PRK03918 693 KKTLEK 698
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
677-1180 |
7.70e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 677 LTRAFERKFNDLEGKLAQAREIVNARnatAEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVQDSNYEASNALSTLER 756
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKE---LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 757 --EAKELNLNSDQLNRQLEILKNsnflgAYDSIRTSYNTSRDAENRANKSATDIpstvsqsADTRKKTERLMsekrddfN 834
Cdd:COG4717 124 llQLLPLYQELEALEAELAELPE-----RLEELEERLEELRELEEELEELEAEL-------AELQEELEELL-------E 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 835 RKNAANKRTLTDLNAKAQlldmkKINEKVADAKTKAQEAKNKAQAALEKASDAKKKvdHSNNDLRDLIKQIREFLMLEGA 914
Cdd:COG4717 185 QLSLATEEELQDLAEELE-----ELQQRLAELEEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLLLLIAAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 915 ------DPDSIEAVANRVLELSI---------PASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKA 979
Cdd:COG4717 258 llallgLGGSLLSLILTIAGVLFlvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 980 RnkAEGVKDTTVSVKQALNDAGKAQAaaekaiekaRNDIGLTQNRLAQIQSETTAQERDldnAMDRLGDLGRQIEALKTK 1059
Cdd:COG4717 338 E--LLELLDRIEELQELLREAEELEE---------ELQLEELEQEIAALLAEAGVEDEE---ELRAALEQAEEYQELKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1060 RanNSLDAARAEETATMARDKANEAKEILDGELsdkyrtvqglmdnkvktmQEAKQKAERLRDEAKELLKDAHDKLQRLE 1139
Cdd:COG4717 404 L--EELEEQLEELLGELEELLEALDEEELEEEL------------------EELEEELEELEEELEELREELAELEAELE 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2516233906 1140 ELEKD--YDENQQVLEGKAKQLDGLEDK---MKAILSAINKKIQIY 1180
Cdd:COG4717 464 QLEEDgeLAELLQELEELKAELRELAEEwaaLKLALELLEEAREEY 509
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1115-1182 |
9.62e-10 |
|
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called epiligrin subunit beta, kalinin B1 chain, kalinin subunit beta, laminin B1k chain, laminin-5 subunit beta, or nicein subunit beta. It is a major component of the basement membrane in most adult tissues. Mutations in LAMB3 are associated with Herlitz junctional epidermolysis bullosa (H-JEB), a severe autosomal recessive disorder characterized by blister formation within the dermal-epidermal basement membrane. LAMB3 is a component of laminin, a complex glycoprotein consisting of three different polypeptide chains (alpha, beta, gamma). Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. This model corresponds to the C-terminal coiled-coil domain of LAMB3, which may be involved in the integrin binding activity.
Pssm-ID: 411974 [Multi-domain] Cd Length: 71 Bit Score: 55.91 E-value: 9.62e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1115 QKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNT 1182
Cdd:cd22303 2 ERVANIKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYST 69
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
653-1178 |
2.10e-09 |
|
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: 62.01 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 653 RIVQDLATRTKALTDRAKELQttgltraferkfnDLEGKLAQAREIVNARNATAEAVTilMGMIEELRGQIGETTETLNQ 732
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEIS-------------ELEKRLEEIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 733 LEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILK--NSNFLGAYDSIRTSYNTSRdaeNRANKSATDIPS 810
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLR---AELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 811 TVSQSADTRKKTERLmSEKRDDFNRknaaNKRTLTDLnakaqlldMKKINEKVADAKtkaqeaknkaqAALEKASDAKKK 890
Cdd:TIGR02169 383 TRDELKDYREKLEKL-KREINELKR----ELDRLQEE--------LQRLSEELADLN-----------AAIAGIEAKINE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 891 VDHSNNDLRDLIKQIREFLMLEGADPDSIEAvanrvlelSIPASPKQIRHLADEIKDRVKSLSNVDA---ILEQTQNDVR 967
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQ--------ELYDLKEEYDRVEKELSKLQRELAEAEAqarASEERVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 968 KAEQLLLD-------------------------AKKARNKAEGVKDTTVSvKQALN-----DAGKAQAaaekaiekarnd 1017
Cdd:TIGR02169 511 AVEEVLKAsiqgvhgtvaqlgsvgeryataievAAGNRLNNVVVEDDAVA-KEAIEllkrrKAGRATF------------ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1018 igLTQNRLAQIQSETTAQERD--LDNAMDrLGDLGRQIE-----ALKTKRANNSLDAARaeetatmaRDKANEAKEILDG 1090
Cdd:TIGR02169 578 --LPLNKMRDERRDLSILSEDgvIGFAVD-LVEFDPKYEpafkyVFGDTLVVEDIEAAR--------RLMGKYRMVTLEG 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1091 ELSDK-------YRTVQGL--------------------MDNKVKTMQEAKQKAERLRDEAKELLKDAHDKL----QRLE 1139
Cdd:TIGR02169 647 ELFEKsgamtggSRAPRGGilfsrsepaelqrlrerlegLKRELSSLQSELRRIENRLDELSQELSDASRKIgeieKEIE 726
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2516233906 1140 ELEKDYDENQQVLEGKAKQLDGLEDKM---KAILSAINKKIQ 1178
Cdd:TIGR02169 727 QLEQEEEKLKERLEELEEDLSSLEQEIenvKSELKELEARIE 768
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1152 |
3.97e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 869 KAQEAKNKAQAAlekasdakKKVDhsnnDLRDLIKQirefLMLEgadPDSIEAVANRVLE----LSipaspkQIRHLADE 944
Cdd:COG4913 192 KALRLLHKTQSF--------KPIG----DLDDFVRE----YMLE---EPDTFEAADALVEhfddLE------RAHEALED 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 945 IKDRVKSLSNVDAI---LEQTQNDVRKAEQLL--LDAKKARNKAEGVKDTTVSVKQALNDAgkaqaaaekaiekarndig 1019
Cdd:COG4913 247 AREQIELLEPIRELaerYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARL------------------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1020 ltQNRLAQIQSETTAQERDLDNAM--------DRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgE 1091
Cdd:COG4913 308 --EAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA-A 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 1092 LSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVL 1152
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
845-1153 |
4.32e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 845 TDLNAKAQLLDMKKINEKVADaKTKAQEAKNKAQAALEKASDA-KKKVDHSNNDLRDLIkQIReflmLEGADPDSIEAVA 923
Cdd:COG3206 81 SPLETQIEILKSRPVLERVVD-KLNLDEDPLGEEASREAAIERlRKNLTVEPVKGSNVI-EIS----YTSPDPELAAAVA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 924 NRVLELSIpaspkqIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKkARNKAEGVKDTTVSVKQALNDAgka 1003
Cdd:COG3206 155 NALAEAYL------EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-QKNGLVDLSEEAKLLLQQLSEL--- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1004 qaaaekaiekaRNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGR--QIEALKTKRANnsLDAARAEETATMARD-- 1079
Cdd:COG3206 225 -----------ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAE--LEAELAELSARYTPNhp 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 1080 ---KANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLE 1153
Cdd:COG3206 292 dviALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
549-590 |
5.02e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 5.02e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2516233906 549 CGCDPNNAYTSACNEFTGQCQCRPGFGGKTCTDCQENHWGNP 590
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
668-1199 |
5.80e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 60.62 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 668 RAKELQTTGLTRAFERKFNDLEGKLAQAREIVNarnataEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVQDSNYEa 747
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWK------EKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 748 snalsTLEREAKELNLNSDQLNRQLEILKNsnFLGAYDSIRTSYNTSRdaENRANKSATDIPSTVSQSADTRKKTERLMS 827
Cdd:pfam12128 341 -----TAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRR--SKIKEQNNRDIAGIKDKLAKIREARDRQLA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 828 EKRDDF--------NRKNAAN-----------------KRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALE 882
Cdd:pfam12128 412 VAEDDLqaleselrEQLEAGKlefneeeyrlksrlgelKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 883 KA-SDAKKKVDHSNNDLRDLIKQIREflmLEGADpdsieavaNRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAileq 961
Cdd:pfam12128 492 SElRQARKRRDQASEALRQASRRLEE---RQSAL--------DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIS---- 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 962 tqndvrkAEQLLldakkaRNKAEGVKDTTvSVKQALNDAGkaqaaaeKAIEKARNDIGLTQNRLAQIQSETTAQERDLDN 1041
Cdd:pfam12128 557 -------PELLH------RTDLDPEVWDG-SVGGELNLYG-------VKLDLKRIDVPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1042 AMDRLGDLGRQIEAlktkrANNSLDAARAEETatMARDKANEAKEILdGELSDKYRTVQglmDNKVKTMQEAKQKA-ERL 1120
Cdd:pfam12128 616 AREKQAAAEEQLVQ-----ANGELEKASREET--FARTALKNARLDL-RRLFDEKQSEK---DKKNKALAERKDSAnERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1121 RDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDG-LEDKMKAILSAINKkiqiyntsgLRLGNDSEMSAQEQQ 1199
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaLDAQLALLKAAIAA---------RRSGAKAELKALETW 755
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
662-1080 |
6.27e-09 |
|
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: 60.51 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 662 TKALTDRAKELQ-TTGLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEGDLTAV 740
Cdd:pfam05483 383 TMELQKKSSELEeMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 741 QDSNYEASNALSTLEREAK-------ELNLNSDQL---NRQLeILKNSNFLGAYDSIRTSYNTSRDAENRANKSATDIPS 810
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEkeklkniELTAHCDKLlleNKEL-TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 811 TVSQSADTRKKTERLMSEKRDDFN---RKNAANKRTLTDLNAKAQllDMKKINEKVADAKTKAQEAKNKAQAALEKASDA 887
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKcklDKSEENARSIEYEVLKKE--KQMKILENKCNNLKKQIENKNKNIEELHQENKA 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 888 KKKVDHSNNdlrdliKQIREFlmlegadpdsiEAVANRvLELSIPASPKQIRHLAD----EIKDrvKSLSNvdailEQTQ 963
Cdd:pfam05483 620 LKKKGSAEN------KQLNAY-----------EIKVNK-LELELASAKQKFEEIIDnyqkEIED--KKISE-----EKLL 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 964 NDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKarNDIGLTQNRLAQIQSETTAQERDLDNAM 1043
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD--SELGLYKNKEQEQSSAKAALEIELSNIK 752
|
410 420 430
....*....|....*....|....*....|....*..
gi 2516233906 1044 DRLGDLGRQIEALKTKRanNSLDAARAEETATMARDK 1080
Cdd:pfam05483 753 AELLSLKKQLEIEKEEK--EKLKMEAKENTAILKDKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
716-1179 |
6.73e-09 |
|
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: 60.42 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 716 IEELRGQIGETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKN---SNFLGAYDS------ 786
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeQDWNKELKSelknqe 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 787 -----IRTSYNTSRDAENRANKSATDIPSTVSQSADTRKKTERLMSEKRD---DFNRKNAANKRTLTDLNAKAQLLDmKK 858
Cdd:TIGR04523 321 kkleeIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeieKLKKENQSYKQEIKNLESQINDLE-SK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 859 INEKVADAKTKAQEAKNKAQA--ALEKA-SDAKKKVDHSNNDLRDLIKQIreflmlegadpdsieavanRVLELSIPASP 935
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEkeLLEKEiERLKETIIKNNSEIKDLTNQD-------------------SVKELIIKNLD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 936 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEG-VKDTTVSVKQALNDAGKaqaaaekaieka 1014
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkVKDLTKKISSLKEKIEK------------ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1015 rndiglTQNRLAQIQSETTAQERDLDNAMDRLGD-------LGRQIEALKTKRANNSLDAARaEETATMARDKANEAKEI 1087
Cdd:TIGR04523 529 ------LESEKKEKESKISDLEDELNKDDFELKKenlekeiDEKNKEIEELKQTQKSLKKKQ-EEKQELIDQKEKEKKDL 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1088 LDgELSDKYRTVqglmDNKVKTMQEAKQKAERLRDEAKElLKDAHDKLQRLEELEKDydenqQVLEGKAKQLDgLEDKMK 1167
Cdd:TIGR04523 602 IK-EIEEKEKKI----SSLEKELEKAKKENEKLSSIIKN-IKSKKNKLKQEVKQIKE-----TIKEIRNKWPE-IIKKIK 669
|
490
....*....|..
gi 2516233906 1168 AILSAINKKIQI 1179
Cdd:TIGR04523 670 ESKTKIDDIIEL 681
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
492-551 |
8.15e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 8.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNLASGrgcEPCGC 551
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE--------TGQCLCKPGVTGRHCDRCKPGYYGLPSD---PPQGC 49
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
709-1198 |
9.88e-09 |
|
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: 60.13 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 709 VTILMGMIEELRGQIgET--TETLNQLEGDLTAVQD------SNYEASnaLSTLEREAKELNLNSDQLNRQLEILKNSnf 780
Cdd:pfam15921 233 ISYLKGRIFPVEDQL-EAlkSESQNKIELLLQQHQDrieqliSEHEVE--ITGLTEKASSARSQANSIQSQLEIIQEQ-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 781 lgaydsirtsyntSRDAENRANKSATDIPSTVSQSADTRKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQLLDMKKIN 860
Cdd:pfam15921 308 -------------ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGN 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 861 EKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRdlIKQIREFLMLEGADPDSIEAVanrvLELSIPASPKQIRH 940
Cdd:pfam15921 375 LDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT--IDHLRRELDDRNMEVQRLEAL----LKAMKSECQGQMER 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 941 LADEIKDRVKSLSNVDAI---LEQTQNDVRKA-EQLLLDAKKARNKAEGVKDTTVSV--KQALNDAGKAQAAAEKAieka 1014
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLtaqLESTKEMLRKVvEELTAKKMTLESSERTVSDLTASLqeKERAIEATNAEITKLRS---- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1015 RNDIGLTQ--------NRLAQIQSETTA-----QERD---------LDNAMDRLGDLGRQIEALKTKRAN--NSLDAARA 1070
Cdd:pfam15921 525 RVDLKLQElqhlknegDHLRNVQTECEAlklqmAEKDkvieilrqqIENMTQLVGQHGRTAGAMQVEKAQleKEINDRRL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1071 E-ETATMARDKANEAKEILDGELSDkyrtvqgLMDNKVKTMQEAKQKAERLRD---EAKELLKDAHDKLQRLEELEKDYD 1146
Cdd:pfam15921 605 ElQEFKILKDKKDAKIRELEARVSD-------LELEKVKLVNAGSERLRAVKDikqERDQLLNEVKTSRNELNSLSEDYE 677
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1147 ENQQVLEGKAKQLDGLEDKMKAILSAINKKI-QIYNTSGLRLGNDSE-----MSAQEQ 1198
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELeQTRNTLKSMEGSDGHamkvaMGMQKQ 735
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
331-370 |
1.00e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNP 370
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1033-1186 |
1.06e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.76 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1033 TAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKVKTMQE 1112
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 1113 AKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAI---LSAINKKIQIYNTSGLR 1186
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAE 182
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
440-485 |
1.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.36 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2516233906 440 CRCSNNIDLSDRgaCDRRTGQCLkCLYNTEGPDCGVCKSGYYGDAS 485
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
331-375 |
1.40e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.97 E-value: 1.40e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNPLISLG 375
Cdd:cd00055 2 CDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
817-1211 |
2.29e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 817 DTRKKTERLMSEKRDDFNRKNAAN-KRTLTDLNAKAQLLD--MKKINEKvadaKTKAQEAKNKAQAALEKASDAKKKVDH 893
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDeeIERYEEQ----REQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 894 SNNDLRDLIKQIREFLMLEGADPDSIEAVANRVLELSipaspKQIRHLADE----------IKDRVKSLSNVDAILEQTQ 963
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELE-----EERDDLLAEaglddadaeaVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 964 NDVRkaeqllLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDLDNAM 1043
Cdd:PRK02224 331 EECR------VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1044 DRLGDLGRQIEALKTKRanNSLDAARAEETATM--ARDKANEAKEILD-GELSDKYRTVQGlmDNKVKTMQEAKQKAERL 1120
Cdd:PRK02224 405 VDLGNAEDFLEELREER--DELREREAELEATLrtARERVEEAEALLEaGKCPECGQPVEG--SPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1121 ---RDEAKELLKDAHDKLQRLEELEKDYDENQQVLEgKAKQLDGLEDKMKAILSAINKKIQIYNTSGLRLgnDSEMSAQE 1197
Cdd:PRK02224 481 eaeLEDLEEEVEEVEERLERAEDLVEAEDRIERLEE-RREDLEELIAERRETIEEKRERAEELRERAAEL--EAEAEEKR 557
|
410
....*....|....
gi 2516233906 1198 QQPSTLTSNAAKIA 1211
Cdd:PRK02224 558 EAAAEAEEEAEEAR 571
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
663-1129 |
2.52e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 663 KALTDRAKELQT-TG-LTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEgdltaV 740
Cdd:COG4717 49 ERLEKEADELFKpQGrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----K 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 741 QDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNsnFLGAYDSIRTSYNTSRDAENRA-NKSATDIPSTVSQSADTR 819
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRE--LEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 820 KKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAK--------------------TKAQEAKNKAQA 879
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 880 ALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRvLELSIPASPKQIRHLADEIKDRVKSLSNVDAIL 959
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA-LGLPPDLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 960 EQ-TQNDVRKAEQLLLDAKKARNKAE-----GVKDTTVSVKQALNDAgKAQAAAEKAIEKARNDIGLT---QNRLAQIQS 1030
Cdd:COG4717 361 EElQLEELEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEEL-EEQLEELLGELEELLEALDEeelEEELEELEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1031 ETTAQERDLDNAMDRLGDLGRQIEALKTkraNNSLDAARAEEtATMARDKANEAKEILdgelsdKYRTVQGLMDnkvKTM 1110
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEE---DGELAELLQEL-EELKAELRELAEEWA------ALKLALELLE---EAR 506
|
490 500
....*....|....*....|
gi 2516233906 1111 QEAKQ-KAERLRDEAKELLK 1129
Cdd:COG4717 507 EEYREeRLPPVLERASEYFS 526
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
492-547 |
2.53e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 2.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNLAS-GRGCE 547
Cdd:cd00055 2 CDCNGHGSLSGQCDPG--------TGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
657-1169 |
2.62e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 657 DLATRTKALTDRAKELQTTGLTRAFERKFNDLEGK-LAQAREIVNARNATAEAVtilmgmIEELRGQIGETTETLNQLEG 735
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEaVEARREELEDRDEELRDR------LEECRVAAQAHNEEAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 736 DLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILknsnflgaydsirtsyntsrDAENRANKSA-TDIPSTVSQ 814
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL--------------------EEEIEELRERfGDAPVDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 815 SADTRKkterLMSEKRDDFNRKNA---ANKRTLTDLNAKAQ-LLDMKKINE--------KVADAKTKAQEAKNKAQAALE 882
Cdd:PRK02224 410 AEDFLE----ELREERDELREREAeleATLRTARERVEEAEaLLEAGKCPEcgqpvegsPHVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 883 KASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRvlelsipaspkqiRHLADEIKDRVKSLSNVDAILEQT 962
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAER-------------RETIEEKRERAEELRERAAELEAE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 963 QNDVRKAeqllldAKKARNKAEGVKDTTvsvkQALNDagkaqaaaekaiekarndigltqnRLAQIQSETTAQERdLDNA 1042
Cdd:PRK02224 553 AEEKREA------AAEAEEEAEEAREEV----AELNS------------------------KLAELKERIESLER-IRTL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1043 MDRLGDLGRQIEALKTKRannsldAARAEetatmardKANEAKEILDgELSDKYRTVQGLMD-NKVKTMQEAKQKAErlr 1121
Cdd:PRK02224 598 LAAIADAEDEIERLREKR------EALAE--------LNDERRERLA-EKRERKRELEAEFDeARIEEAREDKERAE--- 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2516233906 1122 deakELLKDAHDKLQRLEElEKDYDENQ-QVLEGKAKQLDGLEDKMKAI 1169
Cdd:PRK02224 660 ----EYLEQVEEKLDELRE-ERDDLQAEiGAVENELEELEELRERREAL 703
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
716-1210 |
2.80e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 716 IEELRGQIGETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNflGAYDSIRTSYNTSR 795
Cdd:PRK01156 199 LENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE--SDLSMELEKNNYYK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 796 DAENRANKSATD--------IPSTVSQSADTRKKTErLMSEKRDDFNRKNAANKRtLTDLNA-KAQLLDMKKINEKVADA 866
Cdd:PRK01156 277 ELEERHMKIINDpvyknrnyINDYFKYKNDIENKKQ-ILSNIDAEINKYHAIIKK-LSVLQKdYNDYIKKKSRYDDLNNQ 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 867 KTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANrvlelsipaspkQIRHLADEIK 946
Cdd:PRK01156 355 ILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN------------EINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 947 DRVKSLSNVDAILEQTQNDVRKAEQLLldakKARNKAEgVKDTTvsvkqaLNDAGkaqaaaekaIEKARNDIGLTQNRLA 1026
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELSRNMEML----NGQSVCP-VCGTT------LGEEK---------SNHIINHYNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1027 QIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNS---LDAARAEETATM--------ARDKANEAKE----ILDGE 1091
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEynkIESARADLEDIKikinelkdKHDKYEEIKNryksLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1092 LSDKYRTVQGLMDNKVKTMQEAKQKAerlRDEAKELLKDAHDKLQRLE-ELEKDYDENQQVLEGKAKQLDGLEDK----- 1165
Cdd:PRK01156 563 LDSKRTSWLNALAVISLIDIETNRSR---SNEIKKQLNDLESRLQEIEiGFPDDKSYIDKSIREIENEANNLNNKyneiq 639
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2516233906 1166 -MKAILSAINKKIQIYNTsglrlgNDSEMSAQEQQPSTLTSNAAKI 1210
Cdd:PRK01156 640 eNKILIEKLRGKIDNYKK------QIAEIDSIIPDLKEITSRINDI 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1023-1178 |
3.81e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1023 NRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILdGELSDkYRTVQGL 1102
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRN-NKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2516233906 1103 MdnkvKTMQEAKQKAERLRDEAKELLKdahdklqRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQ 1178
Cdd:COG1579 95 Q----KEIESLKRRISDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-1044 |
8.09e-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: 56.99 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 728 ETLNQLE---GDLTAVQDSNYEASNALSTLEREA------KELnlnSDQLNR-QLEILKNSnflgaYDSIRTSYNTSRDA 797
Cdd:TIGR02168 176 ETERKLErtrENLDRLEDILNELERQLKSLERQAekaeryKEL---KAELRElELALLVLR-----LEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 798 ENRANksaTDIPSTVSQSADTRKKTERLMSEKRDDFNRKNAANKRtLTDLNAKAQLLDMKK--INEKVADAKTKA----- 870
Cdd:TIGR02168 248 LKEAE---EELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-LYALANEISRLEQQKqiLRERLANLERQLeelea 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 871 --QEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLML-------EGADPDSIEAVANRVLELSipaspKQIRHL 941
Cdd:TIGR02168 324 qlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrLEELEEQLETLRSKVAQLE-----LQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 942 ADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKA--EGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIG 1019
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAelEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340
....*....|....*....|....*
gi 2516233906 1020 LTQNRLAQIQSETTAQERDLDNAMD 1044
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEG 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
682-925 |
1.02e-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: 55.54 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 682 ERKFNDLEGKLAQAREIVNARNATAEAvtiLMGMIEELRGQIGETTETLNQLEGDLTAvqdsnyeasnalstLEREAKEL 761
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQELAA--------------LEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 762 NLNSDQLNRQLEILKN--SNFLGA-YDSIRTSY-------NTSRDAENRANKSATDIPSTVSQSADTRKKTERLmSEKRD 831
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRAlYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-AALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 832 DFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAAlEKASDAKkkvdhsnnDLRDLIKQIREFLML 911
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAE--------ELEALIARLEAEAAA 238
|
250
....*....|....
gi 2516233906 912 EGADPDSIEAVANR 925
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
492-546 |
1.50e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 1.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2516233906 492 CTCNFLGTERSQCQSRdecvcqrtTGQCQCLPHIIGQTCDHCVPNYWNlASGRGC 546
Cdd:smart00180 1 CDCDPGGSASGTCDPD--------TGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
663-1178 |
2.73e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 663 KALTDRAKELQTTgltrafERKFNDLEGKLAQAR-EIVNARNATAEavtilmGMIEELRGQIGETTETLNQLEGDLTAVQ 741
Cdd:TIGR04523 267 KQLSEKQKELEQN------NKKIKELEKQLNQLKsEISDLNNQKEQ------DWNKELKSELKNQEKKLEEIQNQISQNN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 742 DSNYEASNALSTLEREAKELNLNSDQLNRQL-------EILKNSNflgaydsirTSYNTS-RDAENRANKSATDIPSTVS 813
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELeekqneiEKLKKEN---------QSYKQEiKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLMSEKR------DDFNRKNAANKRTLTDLNAKAQLLDmKKINEkvADAKTKAQEAK--------NKAQA 879
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKEllekeiERLKETIIKNNSEIKDLTNQDSVKE-LIIKN--LDNTRESLETQlkvlsrsiNKIKQ 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 880 ALEKasdAKKKVDHSNNDLRDLIKQIREflmLEGadpdsieavANRVLELSIPASPKQIRHLADEIKDRVKSLSNVDAIL 959
Cdd:TIGR04523 483 NLEQ---KQKELKSKEKELKKLNEEKKE---LEE---------KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 960 EqTQNDVRKAEQLlldakkarnkaEGVKDttvsvkqalndaGKAQAAaekaiekarNDIGLTQNRLAQIQSEttaQERDL 1039
Cdd:TIGR04523 548 N-KDDFELKKENL-----------EKEID------------EKNKEI---------EELKQTQKSLKKKQEE---KQELI 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1040 DNAMDRLGDLGRQIEALKTKRAN--NSLDAARAE-ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQK 1116
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKISSleKELEKAKKEnEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2516233906 1117 AERLrDEAKELLKD------AHDK--------LQRLEELEKDYDENQQVLegkaKQLDGLEDKMKAILSAINKKIQ 1178
Cdd:TIGR04523 672 KTKI-DDIIELMKDwlkelsLHYKkyitrmirIKDLPKLEEKYKEIEKEL----KKLDEFSKELENIIKNFNKKFD 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
655-1168 |
2.74e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 655 VQDLATRTKALTDRAKELQTTGLTRAF---ERKFNDLEGKLAQAREivnARNATAEAVTILMGMIEELRGQIGETTETLN 731
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLwfaQRRLELLEAELEELRA---ELARLEAELERLEARLDALREELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 732 QLEGDLTAvqdsnyEASNALSTLEREAKELNLNSDQLNRQLEILKnsnfLGAYDSIRTSYNTSRDAENRANKSAtdipst 811
Cdd:COG4913 334 GNGGDRLE------QLEREIERLERELEERERRRARLEALLAALG----LPLPASAEEFAALRAEAAALLEALE------ 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 812 vSQSADTRKKTERLMSEKRDDFNRKNAANKRtLTDLNAK-----AQLLDMKK-INEKVADAKTKAQ--------EAKNKA 877
Cdd:COG4913 398 -EELEALEEALAEAEAALRDLRRELRELEAE-IASLERRksnipARLLALRDaLAEALGLDEAELPfvgelievRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 878 -QAALEKA---------------SDAKKKVDhsNNDLR-----DLIKQIREFLMLEGADPDSIeavanrVLELSIPASP- 935
Cdd:COG4913 476 wRGAIERVlggfaltllvppehyAAALRWVN--RLHLRgrlvyERVRTGLPDPERPRLDPDSL------AGKLDFKPHPf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 936 -----KQIRHLAD------------------------------EIKDRVKSLSN----VDAI--LEQTQNDVRKAEQLLL 974
Cdd:COG4913 548 rawleAELGRRFDyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRIRSRyvlgFDNRakLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 975 DAKKARNKAEGVKDTTVSVKQALNDAGKAQAAaekaiekaRNDIGLTQNRLAQIQsettAQERDLDNAMDRLGDLGRQIE 1054
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEYSWD--------EIDVASAEREIAELE----AELERLDASSDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1055 ALKTKrannsLDAARAEetatmaRDKANEAKEILDGELSDKYRTVQGLMDNKVktmQEAKQKAERLRDEAKELLKDAHDK 1134
Cdd:COG4913 696 ELEAE-----LEELEEE------LDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAAALGD 761
|
570 580 590
....*....|....*....|....*....|....*
gi 2516233906 1135 lQRLEELEKDYDENQQVLEGKAKQL-DGLEDKMKA 1168
Cdd:COG4913 762 -AVERELRENLEERIDALRARLNRAeEELERAMRA 795
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
439-490 |
3.07e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.12 E-value: 3.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2516233906 439 SCRCSNNIDLSDRgaCDRRTGQCLkCLYNTEGPDCGVCKSGYYGDASRRN-CR 490
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGgCQ 50
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
959-1178 |
5.47e-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: 54.30 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 959 LEQTQNDVRKAEQLLLDAKKARNKAEGVKDttvSVKQALNDAGKaqaaaekaiekarnDIGLTQNRLAQIQSETTAQERD 1038
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASR--------------KIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1039 LDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAK--------EILDGELSDKYRTVQGL------MD 1104
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsriPEIQAELSKLEEEVSRIearlreIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1105 NKVKTMQEAKQKAERLRDEAKELLKDAHDKL----QRLEELEKDYDENQQVLEGKAKQLDGLE----------DKMKAIL 1170
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAALRDLEsrlgdlkkerDELEAQL 898
|
....*...
gi 2516233906 1171 SAINKKIQ 1178
Cdd:TIGR02169 899 RELERKIE 906
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
380-438 |
6.41e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 47.35 E-value: 6.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 380 PCPCPEGPSSGrhfaATCYQDNrnqqVVCNCNQGYTGSRCEECASGYYGNPSQPGGrCQ 438
Cdd:cd00055 1 PCDCNGHGSLS----GQCDPGT----GQCECKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
381-437 |
8.74e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 8.74e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2516233906 381 CPCPEGPSSGrhfaATCYQdnrnQQVVCNCNQGYTGSRCEECASGYYGNPSQPGGRC 437
Cdd:pfam00053 1 CDCNPHGSLS----DTCDP----ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
331-370 |
9.32e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 9.32e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2516233906 331 CQCNGQ---TEECHQRTGACLnCRGNTAGDKCERCANGYHGNP 370
Cdd:smart00180 1 CDCDPGgsaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
663-954 |
9.42e-07 |
|
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: 53.04 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 663 KALTDRAKELQTTGLTRAFERKFNDLEGKL-AQAREIVNARNATAEAVTILMGMIEELRG--QIGETTETLNQL------ 733
Cdd:COG5185 309 KATESLEEQLAAAEAEQELEESKRETETGIqNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDSFkdties 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 --EGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNFlgaydsirTSYNTSRDAENRANKSATDIPST 811
Cdd:COG5185 389 tkESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE--------EVSKLLNELISELNKVMREADEE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 812 VSQSADTR-KKTERLMSEKRDDFNRK-NAANKRTLTDLNAKAQLLDmkKINEKVADAKTKAQEAKNKAQAALEKASDAKK 889
Cdd:COG5185 461 SQSRLEEAyDEINRSVRSKKEDLNEElTQIESRVSTLKATLEKLRA--KLERQLEGVRSKLDQVAESLKDFMRARGYAHI 538
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2516233906 890 KVDhsNNDLRDLIKQirEFLMLEgaDPDSIEAVANRVLElsipaSPKQIRHLADEIKDRVKSLSN 954
Cdd:COG5185 539 LAL--ENLIPASELI--QASNAK--TDGQAANLRTAVID-----ELTQYLSTIESQQAREDPIPD 592
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
810-1078 |
1.57e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 810 STVSQSADTrkKTERLMSEKRDDFNRKNAANKRtLTDLNAKAQlldmkKINEKVADAKTKAQEAKNKAQAALEKASDAKK 889
Cdd:COG3883 8 APTPAFADP--QIQAKQKELSELQAELEAAQAE-LDALQAELE-----ELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 890 KVDHSNNDLRDLIKQIRE-------FLMLEGADpdSIEAVANRVLELSIPASpkQIRHLADEIKDRVKSLSNVDAILEQT 962
Cdd:COG3883 80 EIEERREELGERARALYRsggsvsyLDVLLGSE--SFSDFLDRLSALSKIAD--ADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 963 QNDVRKAEQLLLDAKKArnkaegvKDTTVSVKQALNDAGKAQAAAEKAIEKARNDigltQNRLAQIQSETTAQERDLDNA 1042
Cdd:COG3883 156 LAELEALKAELEAAKAE-------LEAQQAEQEALLAQLSAEEAAAEAQLAELEA----ELAAAEAAAAAAAAAAAAAAA 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 2516233906 1043 MDRLGDLGRQIEALKTKRANNSLDAARAEETATMAR 1078
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAG 260
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
789-1167 |
2.20e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 789 TSYNTSRDAENRANKSA----TDIPSTVSQSADTRKKTERLmsekrdDFNRKNAANKRT-LTDLNA-----KAQLL---- 854
Cdd:NF033838 47 TVTSSGNESQKEHAKEVeshlEKILSEIQKSLDKRKHTQNV------ALNKKLSDIKTEyLYELNVlkeksEAELTsktk 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 855 ------------DMKKINEKVADAKTKAQEAKNKAQAALEKasdakkkvdhsnnDLRDLIKQIREFLMLEGADPDSieAV 922
Cdd:NF033838 121 keldaafeqfkkDTLEPGKKVAEATKKVEEAEKKAKDQKEE-------------DRRNYPTNTYKTLELEIAESDV--EV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 923 ANRVLELsipaspkqIRHLADEIKDRVKsLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDttVSVKQALNDAGK 1002
Cdd:NF033838 186 KKAELEL--------VKEEAKEPRDEEK-IKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRAD--AKLKEAVEKNVA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1003 AQAAAEKAIEKARNDIGltqnrlaqIQSETTAQERDLDNAMDRLGDlgrqiEALKTKRANNSLDAARAEETATMARDKAN 1082
Cdd:NF033838 255 TSEQDKPKRRAKRGVLG--------EPATPDKKENDAKSSDSSVGE-----ETLPSPSLKPEKKVAEAEKKVEEAKKKAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1083 EAKEildgelSDK-------YRTVQ---GLMDNKVKtmqeaKQKAERLRDEAK-----ELLKDAHDKLQ-------RLEE 1140
Cdd:NF033838 322 DQKE------EDRrnyptntYKTLEleiAESDVKVK-----EAELELVKEEAKeprneEKIKQAKAKVEskkaeatRLEK 390
|
410 420
....*....|....*....|....*..
gi 2516233906 1141 LEKDydenQQVLEGKAKQLDGLEDKMK 1167
Cdd:NF033838 391 IKTD----RKKAEEEAKRKAAEEDKVK 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
808-1080 |
2.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 808 IPSTVSQSADTRKKTERLMSEKRDDFNRKNAANKRTLTDlnAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDA 887
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE--EKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 888 KKKVDHSNNDLRDLIKQIREFL--MLEGADPDSIEAVANrvlelsiPASPKQ-------IRHLADEIKDRVKSLSNVDAI 958
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLLS-------PEDFLDavrrlqyLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 959 LEQTQNDVrKAEQLLLDAKKARNKAEgvkdttvsvKQALNDAGKAQaaaekaiekarndigltQNRLAQIQSETTAQERD 1038
Cdd:COG4942 162 LAALRAEL-EAERAELEALLAELEEE---------RAALEALKAER-----------------QKLLARLEKELAELAAE 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2516233906 1039 LDNAMDRLGDLGRQIEALKTKRAnnslDAARAEETATMARDK 1080
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAA----AAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1015-1222 |
2.44e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1015 RNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSD 1094
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KYRT-----VQGLMDNK-----VKTMQEAKQKAERLRDEAKEL---LKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDG 1161
Cdd:COG4942 113 LYRLgrqppLALLLSPEdfldaVRRLQYLKYLAPARREQAEELradLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 1162 LEDKMKAILSAINKKIQIYNtsglrlgndSEMSAQEQQPSTLTSNAAKIAGPGRKRHNSDP 1222
Cdd:COG4942 193 LKAERQKLLARLEKELAELA---------AELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
682-1160 |
3.22e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 682 ERKFNDLEGKLAQAREivNARNATAEAVTILMGMIEELRGQIGETTETLNqlegdltavqdsnyeaSNALstlereaKEL 761
Cdd:TIGR01612 1025 EKATNDIEQKIEDANK--NIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN----------------KEIL-------EEA 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 762 NLNSDQLNRQLEILKNSNF--LGAYDSIRTSyntsrdaeNRANKSATDIpSTVSQSAD--------TRKKTERLMSEKRD 831
Cdd:TIGR01612 1080 EINITNFNEIKEKLKHYNFddFGKEENIKYA--------DEINKIKDDI-KNLDQKIDhhikaleeIKKKSENYIDEIKA 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 832 DFNRKNAANKRTL----------------TDLNAKAQLLD-MKK-INE--KVADAKTKAQEAKNKAQAA--------LEK 883
Cdd:TIGR01612 1151 QINDLEDVADKAIsnddpeeiekkienivTKIDKKKNIYDeIKKlLNEiaEIEKDKTSLEEVKGINLSYgknlgklfLEK 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 884 ASDAKKKVDHSNNDLRDLIKQIREF--LMLEGADPDSIEAVANRVLE-LSIPASPKQIRHLADE-----IKD-RVKSLSN 954
Cdd:TIGR01612 1231 IDEEKKKSEHMIKAMEAYIEDLDEIkeKSPEIENEMGIEMDIKAEMEtFNISHDDDKDHHIISKkhdenISDiREKSLKI 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 955 VDAILEQTQ-NDVRKAEQL-LLDAKKARN----------------KAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKA-- 1014
Cdd:TIGR01612 1311 IEDFSEESDiNDIKKELQKnLLDAQKHNSdinlylneianiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSek 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1015 -----RNDIGLTQnrlAQIQSETTAQERDLDNAMDRLGDLGRQIealKTKRANNSLDAARAEE----------TATMARD 1079
Cdd:TIGR01612 1391 likkiKDDINLEE---CKSKIESTLDDKDIDECIKKIKELKNHI---LSEESNIDTYFKNADEnnenvlllfkNIEMADN 1464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1080 KANEAKEIL-DGELSDkyrtvqglMDNKVKTMQEAKQKAERLRDEAKELLKdahdKLQRLEELEKDYDENQQVLEGKAKQ 1158
Cdd:TIGR01612 1465 KSQHILKIKkDNATND--------HDFNINELKEHIDKSKGCKDEADKNAK----AIEKNKELFEQYKKDVTELLNKYSA 1532
|
..
gi 2516233906 1159 LD 1160
Cdd:TIGR01612 1533 LA 1534
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1048-1198 |
3.29e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1048 DLGRQIEALKTKRANN-----SLDAARAEETATMARDKANEAKEILDGELsDKYRTVQGLMDNKVKTMQEAKQKAERLRD 1122
Cdd:PRK04778 253 DIEKEIQDLKEQIDENlalleELDLDEAEEKNEEIQERIDQLYDILEREV-KARKYVEKNSDTLPDFLEHAKEQNKELKE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1123 EAkELLKD----AHDKLQ-------RLEELEKDYDENQQVLEGKAKQLDGLEDKMKAI---LSAINKK-IQIYNT-SGLR 1186
Cdd:PRK04778 332 EI-DRVKQsytlNESELEsvrqlekQLESLEKQYDEITERIAEQEIAYSELQEELEEIlkqLEEIEKEqEKLSEMlQGLR 410
|
170
....*....|..
gi 2516233906 1187 lgnDSEMSAQEQ 1198
Cdd:PRK04778 411 ---KDELEAREK 419
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
848-1145 |
3.58e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 848 NAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRVL 927
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 928 ELSipaspKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAa 1007
Cdd:COG4372 112 ELQ-----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1008 ekaiekarNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKT-KRANNSLDAARAEETATMARDKANEAKE 1086
Cdd:COG4372 186 --------DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEaKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1087 ILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDY 1145
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1016-1176 |
4.66e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 48.75 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1016 NDIglTQNRLAQIQSettaqerdldnamdrlgdLGRQIEALKTKRANNS--LDAARAE-----ETATMARDKANEAKEIL 1088
Cdd:pfam13851 18 NDI--TRNNLELIKS------------------LKEEIAELKKKEERNEklMSEIQQEnkrltEPLQKAQEEVEELRKQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1089 DGELSDKyrtvqglmdnkvKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDE-----NQQVLE-----GKAKQ 1158
Cdd:pfam13851 78 ENYEKDK------------QSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfEAAIQDvqqktGLKNL 145
|
170
....*....|....*...
gi 2516233906 1159 LdgLEDKMKAILSAINKK 1176
Cdd:pfam13851 146 L--LEKKLQALGETLEKK 161
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
668-1175 |
4.74e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 668 RAK-ELQTTGLTRAFERKFNDLEGKLAQAREivnaRNATAeavtilmgmIEELRGQIGETTETLNQLEGDLTAVQDSNYE 746
Cdd:pfam01576 322 RSKrEQEVTELKKALEEETRSHEAQLQEMRQ----KHTQA---------LEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 747 ASNALSTL--------------EREAKELNLNSDQLNRQLEIL--KNSNFLGAYDSIRTSYNtsrDAENRANKSATDIPS 810
Cdd:pfam01576 389 LQAELRTLqqakqdsehkrkklEGQLQELQARLSESERQRAELaeKLSKLQSELESVSSLLN---EAEGKNIKLSKDVSS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 811 TVSQSADTRkktERLMSEKRDDFN----------RKNA---------ANKRTLTD--LNAKAQLLDMKKINEKVADAKTK 869
Cdd:pfam01576 466 LESQLQDTQ---ELLQEETRQKLNlstrlrqledERNSlqeqleeeeEAKRNVERqlSTLQAQLSDMKKKLEEDAGTLEA 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 870 AQEAKNKAQaalekasdakkkvdhsnNDLRDLIKQIREflmlEGADPDSIEAVANRvlelsipaspkqirhLADEIKDRV 949
Cdd:pfam01576 543 LEEGKKRLQ-----------------RELEALTQQLEE----KAAAYDKLEKTKNR---------------LQQELDDLL 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 950 KSLSNVDAILEQTQNDVRKAEQLLLDAKKA-------RNKAEG---VKDTTV-SVKQALNDAGKAQAAAEKaiekarndi 1018
Cdd:pfam01576 587 VDLDHQRQLVSNLEKKQKKFDQMLAEEKAIsaryaeeRDRAEAearEKETRAlSLARALEEALEAKEELER--------- 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1019 gltQNRLAQIQSEttaqerDLDNAMDrlgDLGRQIEAL-KTKRAnnsldaaraeetatmARDKANEAKEILDgELSDKyr 1097
Cdd:pfam01576 658 ---TNKQLRAEME------DLVSSKD---DVGKNVHELeRSKRA---------------LEQQVEEMKTQLE-ELEDE-- 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1098 tVQGLMDNKVK---TMQEAKQKAER---LRDEAKE-----LLKDAHDklqrLE-ELEKDYDENQQVLEGKaKQLDGLEDK 1165
Cdd:pfam01576 708 -LQATEDAKLRlevNMQALKAQFERdlqARDEQGEekrrqLVKQVRE----LEaELEDERKQRAQAVAAK-KKLELDLKE 781
|
570
....*....|
gi 2516233906 1166 MKAILSAINK 1175
Cdd:pfam01576 782 LEAQIDAANK 791
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
653-1203 |
7.52e-06 |
|
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: 50.43 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 653 RIVQDLATRTKALTDRAKELQTTGLTRAFERKFNDL-----------EGKLAQAREIVNARNATAEAVTILMGMIEELRG 721
Cdd:TIGR00606 183 RYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKaceirdqitskEAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 722 QIGETTETLNQLEGDLTAVQDSNYEAS------------------------------------NALSTLEREAKELN--- 762
Cdd:TIGR00606 263 KIMKLDNEIKALKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqrtvrekerelvdcqRELEKLNKERRLLNqek 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 763 --LNSDQLNRQLEILKNSNFLGAYDSIRTSYNTSR--DAENRANKSATDIPSTVSQSADTRKKTERLMSEKRDDFNRKNA 838
Cdd:TIGR00606 343 teLLVEQGRLQLQADRHQEHIRARDSLIQSLATRLelDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 839 ANKRTLTDLNAKAQLLDMKKINEKVADAKtKAQEAKNKAQAA--LEKASDAKKKVDhsnndlRDLIKQIREflmLEGADP 916
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEILEK-KQEELKFVIKELqqLEGSSDRILELD------QELRKAERE---LSKAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 917 DSieavanrvlelSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKD-----TTV 991
Cdd:TIGR00606 493 NS-----------LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhSDE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 992 SVKQALNDAGKAQAAAEKAIEkaRNDIGLTQNRLAQIQSETTAQERDLDNAMDRLgdlgRQIEALKTKRANNSLDAARAE 1071
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSK--SKEINQTRDRLAKLNKELASLEQNKNHINNEL----ESKEEQLSSYEDKLFDVCGSQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1072 -ETATMAR-----DKANEAKEILDG----------ELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDeakeLLKDAHDKL 1135
Cdd:TIGR00606 636 dEESDLERlkeeiEKSSKQRAMLAGatavysqfitQLTDENQSCCPVCQRVFQTEAELQEFISDLQS----KLRLAPDKL 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516233906 1136 QRLE----ELEKDYDENQQVLEGKAKQLDGLEDKMKailsAINKKIQIYNTSGLRLGNDseMSAQEQQPSTL 1203
Cdd:TIGR00606 712 KSTEselkKKEKRRDEMLGLAPGRQSIIDLKEKEIP----ELRNKLQKVNRDIQRLKND--IEEQETLLGTI 777
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
658-1169 |
8.95e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 658 LATRTKALTDRAKELQT-----TGLTRAFERKFNDLEGKLAQAREIVNARNATAEAV----TILMGMIEELRGQIGETTE 728
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEqleeeEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkKRLQRELEALTQQLEEKAA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 729 TLNQLE----------GDLTAVQDSNYEAsnaLSTLEREAKELnlnsDQLnrqleilknsnfLGAYDSIRTSYNTSRDae 798
Cdd:pfam01576 567 AYDKLEktknrlqqelDDLLVDLDHQRQL---VSNLEKKQKKF----DQM------------LAEEKAISARYAEERD-- 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 799 nRAnksatdipstvsqSADTRKKTERLMS---------EKRDDFNRKNAANKRTLTDL-NAK------------------ 850
Cdd:pfam01576 626 -RA-------------EAEAREKETRALSlaraleealEAKEELERTNKQLRAEMEDLvSSKddvgknvhelerskrale 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 851 AQLLDMKKINEKVADAKTKAQEAKNKAQAALEkASDAKKKVDHSNND------LRDLIKQIREF-LMLEGADPDSIEAVA 923
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQ-ALKAQFERDLQARDeqgeekRRQLVKQVRELeAELEDERKQRAQAVA 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 924 NRV--------LELSIPASP-------KQIRHLADEIKDRVKSLSNV----DAILEQTQNDVRKAEQL----------LL 974
Cdd:pfam01576 771 AKKkleldlkeLEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEArasrDEILAQSKESEKKLKNLeaellqlqedLA 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 975 DAKKARNKAEGVKDTtVSVKQALNDAGKAqaaaekaieKARNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIE 1054
Cdd:pfam01576 851 ASERARRQAQQERDE-LADEIASGASGKS---------ALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVE 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1055 ALKTKRANNSLDAARAEETATMARDKANEAKEIL---DGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDA 1131
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLqemEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRT 1000
|
570 580 590
....*....|....*....|....*....|....*...
gi 2516233906 1132 HDKLQrleELEKDYDENQQVLEGKAKQLDGLEDKMKAI 1169
Cdd:pfam01576 1001 EKKLK---EVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1015-1179 |
9.35e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1015 RNDIGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALktkraNNSLDAARAEETATMAR-DKANEAKEILDGELs 1093
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL-----NEQLQAAQAELAQAQEElESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1094 dkyrtvqglmdNKVKT-MQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLED-----KMK 1167
Cdd:COG4372 118 -----------EELQKeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEaeaeqALD 186
|
170
....*....|..
gi 2516233906 1168 AILSAINKKIQI 1179
Cdd:COG4372 187 ELLKEANRNAEK 198
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-921 |
1.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 716 IEELRGQIGETTETLNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQL-----EILKNSNFLGayDSIRTS 790
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeaEIEERREELG--ERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 791 YNTSRDaenranksaTDIPSTVSQSADTrkkterlmsekrDDFNRkNAANKRTLTDLNAKAqLLDMKKINEKVADAKTKA 870
Cdd:COG3883 96 YRSGGS---------VSYLDVLLGSESF------------SDFLD-RLSALSKIADADADL-LEELKADKAELEAKKAEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 871 QEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEA 921
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
696-1199 |
1.46e-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: 49.40 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 696 REIVNARNATAEavtiLMGMIEELRGQIG----ETTETLNQLE---GDLTAVQDSNYEASNALSTL----EREAKELNLN 764
Cdd:pfam01576 215 GESTDLQEQIAE----LQAQIAELRAQLAkkeeELQAALARLEeetAQKNNALKKIRELEAQISELqedlESERAARNKA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 765 SDQ---LNRQLEILKnSNFLGAYDSIRTS--YNTSRDAENRANKSATDIPSTV--SQSADTRKK-TERL--MSEKRDDFN 834
Cdd:pfam01576 291 EKQrrdLGEELEALK-TELEDTLDTTAAQqeLRSKREQEVTELKKALEEETRSheAQLQEMRQKhTQALeeLTEQLEQAK 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 835 RKNAA---NKRTL----TDLNAKAQLLDM---------KKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDL 898
Cdd:pfam01576 370 RNKANlekAKQALesenAELQAELRTLQQakqdsehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 899 RDLIKQIREFlmleGADPDSIEAVANRVLELsipaspkqirhLADEIKDRVKSLSNVDAiLEQTQNDVRkaEQLLLDAKK 978
Cdd:pfam01576 450 NEAEGKNIKL----SKDVSSLESQLQDTQEL-----------LQEETRQKLNLSTRLRQ-LEDERNSLQ--EQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 979 ARNKAEGVKDTTVSV----KQALNDAGKAQAAAEKAIEKARNDIGLTQnrlaQIQSETTAQERdLDNAMDRLG------- 1047
Cdd:pfam01576 512 KRNVERQLSTLQAQLsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQ----QLEEKAAAYDK-LEKTKNRLQqelddll 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1048 -DLGRQ---IEALKTKRanNSLDAARAEETATMA-----RDKAN-EAKEILDGELSdkyrtvqglMDNKVKTMQEAKQKA 1117
Cdd:pfam01576 587 vDLDHQrqlVSNLEKKQ--KKFDQMLAEEKAISAryaeeRDRAEaEAREKETRALS---------LARALEEALEAKEEL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1118 ER----LRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAilsAINKKIQI-YNTSGLRLGNDSE 1192
Cdd:pfam01576 656 ERtnkqLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLeVNMQALKAQFERD 732
|
....*..
gi 2516233906 1193 MSAQEQQ 1199
Cdd:pfam01576 733 LQARDEQ 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
827-1176 |
2.32e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 827 SEKRDDFNRKNAaNKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAAlEKASDAKKKVDhsnndlrdlIKQIR 906
Cdd:PTZ00121 1075 SYKDFDFDAKED-NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA-RKAEEARKAED---------ARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 907 EflmLEGADPDSIEAVANRVLElsipASPKQIRHLADEIKdrvKSLSNVDAILEQTQNDVRKAEqlllDAKKAR--NKAE 984
Cdd:PTZ00121 1144 E---ARKAEDAKRVEIARKAED----ARKAEEARKAEDAK---KAEAARKAEEVRKAEELRKAE----DARKAEaaRKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 985 GVKDTTvSVKQAlNDAGKAQAAAEKAIEKARNDigltQNRLAQiqsETTAQERDLDNAMDRLGDLGRQIEALKTKRANNS 1064
Cdd:PTZ00121 1210 EERKAE-EARKA-EDAKKAEAVKKAEEAKKDAE----EAKKAE---EERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1065 LDAARAEETATMarDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKD 1144
Cdd:PTZ00121 1281 DELKKAEEKKKA--DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
330 340 350
....*....|....*....|....*....|..
gi 2516233906 1145 YDENQQvlEGKAKQLDGLEDKMKAilSAINKK 1176
Cdd:PTZ00121 1359 AEAAEE--KAEAAEKKKEEAKKKA--DAAKKK 1386
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-1065 |
2.73e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 657 DLATRTKALTDRAKELQTTGLTR--AFERKFNDLEGKLAQAREIVNARNATaeavtilmgmIEELRGQIGETTETLNQLE 734
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFEldKLQEELEQLREELEQAREELEQLEEE----------LEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 735 GDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKnsnflgaydsirtsyntsrDAENRANKSATDIPSTVSQ 814
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE-------------------QQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 815 sadtrkKTERLmsekrDDFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEkasdakkkvdhs 894
Cdd:COG4372 148 ------REEEL-----KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 895 nnDLRDLIKQIREFLMLEGADPDSIEAVANRVLELSIPASPKQIrhlADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLL 974
Cdd:COG4372 205 --AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE---DKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 975 DAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQErDLDNAMDRLGDLGRQIE 1054
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD-LLQLLLVGLLDNDVLEL 358
|
410
....*....|.
gi 2516233906 1055 ALKTKRANNSL 1065
Cdd:COG4372 359 LSKGAEAGVAD 369
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
880-1181 |
3.62e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 880 ALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRVLELSipaspKQIRHLADEikdrvkslsnvdail 959
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS-----SELPELREE--------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 960 eqtqndVRKAEQLLLDAKKARNKAEGVKdttvsvkqalndagkaqaaaekaiekarndigltqNRLAQIQSETTAQERDL 1039
Cdd:PRK03918 223 ------LEKLEKEVKELEELKEEIEELE-----------------------------------KELESLEGSKRKLEEKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1040 DNAMDRLGDLGRQIEALKtkrannsldaaraeetatmarDKANEAKEIldGELSDKYRTVQGLMDNKVKTMQEAKQKAER 1119
Cdd:PRK03918 262 RELEERIEELKKEIEELE---------------------EKVKELKEL--KEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1120 LRDEAKEL---LKDAHDKLQRLEELEKDYDENQQ---VLEGKAKQLDGLEDKMKAiLSAINKKIQIYN 1181
Cdd:PRK03918 319 LEEEINGIeerIKELEEKEERLEELKKKLKELEKrleELEERHELYEEAKAKKEE-LERLKKRLTGLT 385
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
440-483 |
3.66e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.30 E-value: 3.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2516233906 440 CRCsnNIDLSDRGACDRRTGQCLkCLYNTEGPDCGVCKSGYYGD 483
Cdd:smart00180 1 CDC--DPGGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| GldM_N |
pfam12081 |
GldM N-terminal domain; This domain is found in bacteria at the N-terminus of the GldM protein. ... |
831-976 |
4.00e-05 |
|
GldM N-terminal domain; This domain is found in bacteria at the N-terminus of the GldM protein. This domain is typically between 169 to 182 amino acids in length. This domain has two completely conserved residues (Y and N) that may be functionally important. GldM, is named for the member from Cytophaga johnsonae (Flavobacterium johnsoniae), which is required for a type of rapid gliding motility found in certain members of the Bacteriodetes.
Pssm-ID: 432316 Cd Length: 186 Bit Score: 45.69 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 831 DDFNRKNAA----NKRTLTDLNAKaqlldMKKINEKVADAKTKAQEAKNKAQ----------AALEKASDAKK--KVDHS 894
Cdd:pfam12081 10 ESLERSNKNasekNDALYASLEAK-----AEENPEKAKEWYDKAKEVKAKSDelynyieslkTEIVREAGGKDgdVGDYK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 895 NNDLRDLIKQIreflMLEGADP------DSIEAVANRVLEL---SIPASPKQIRHLADEIKDRVKSlsNVD--------- 956
Cdd:pfam12081 85 NKDDLDAADEV----MLNPYSGkgkelrKKINEYREEVLKLvgdKIAKDRKESNLSTEDPKDKDGK--NKDweeynfegf 158
|
170 180
....*....|....*....|....*.
gi 2516233906 957 ------AILEQTQNDVRKAEQLLLDA 976
Cdd:pfam12081 159 plvaalTKLSKLQSDVRNAESEVLHT 184
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
381-430 |
5.99e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 5.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2516233906 381 CPCPegpsSGRHFAATCYQDNrnqqVVCNCNQGYTGSRCEECASGYYGNP 430
Cdd:smart00180 1 CDCD----PGGSASGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1023-1168 |
6.04e-05 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 45.81 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1023 NRLAQIQSETTAQERDLDNAMdrlGDLGR------QIEALKTKRANNSLD--AARAEETATMARDKANEAKEILDGELSD 1094
Cdd:cd07596 21 KKLSKQAQRLVKRRRELGSAL---GEFGKaliklaKCEEEVGGELGEALSklGKAAEELSSLSEAQANQELVKLLEPLKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1095 KYRTVQGLMD------NKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKA 1168
Cdd:cd07596 98 YLRYCQAVKEtlddraDALLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRYEEISERLKE 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
685-1173 |
6.79e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 685 FNDLEGklAQaREIVNARnataEAVTILmGMIEELRGQIGETTETLNQLEGDLTAVQDsnYEASNALSTLEREAKELNLN 764
Cdd:COG4913 234 FDDLER--AH-EALEDAR----EQIELL-EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 765 SDQLNRQLEILKNsnflgAYDSIRTSYntsRDAENRANKSATDIPSTVSQSADTRKKTERLMSEKRDDFNR-------KN 837
Cdd:COG4913 304 LARLEAELERLEA-----RLDALREEL---DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaalglPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 838 AANKRTLTDL--NAKAQLLDMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNN----DLRDLIKQIREFLML 911
Cdd:COG4913 376 PASAEEFAALraEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 912 EGADP-----------------DSIEAV-ANRVLELSIPAspkqiRHLAD--EIKDRVKSLSNVD--AILEQTQNDVRK- 968
Cdd:COG4913 456 DEAELpfvgelievrpeeerwrGAIERVlGGFALTLLVPP-----EHYAAalRWVNRLHLRGRLVyeRVRTGLPDPERPr 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 969 ------AEQLLLDAKKARNKAEG--------VKDTTVsvkQALNDAGKAqaaaekaiekarndigLTQNRlaQIQSETTA 1034
Cdd:COG4913 531 ldpdslAGKLDFKPHPFRAWLEAelgrrfdyVCVDSP---EELRRHPRA----------------ITRAG--QVKGNGTR 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1035 QERDLDNAMDR---LG-DLGRQIEALKTKRAnnsldaaRAEETATMARDKANEAKEILDG--ELSDKYRTVQGLMDNKVK 1108
Cdd:COG4913 590 HEKDDRRRIRSryvLGfDNRAKLAALEAELA-------ELEEELAEAEERLEALEAELDAlqERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1109 tMQEAKQKAERLRDEaKELLKDAHDKL----QRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAI 1173
Cdd:COG4913 663 -VASAEREIAELEAE-LERLDASSDDLaaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
659-1195 |
1.14e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 659 ATRTKALTDRAKELQTTGLTRAFERKFNDLEGKLAQAREIVNarNATAEAVTILMGMIEE---LRGQIGETTETLN-QLE 734
Cdd:NF041483 555 ARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA--DARAEAERIRREAAEEterLRTEAAERIRTLQaQAE 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 735 GDLTAVQD-SNYEASNALStlEREAKELNLNSDQLNrQLEILKNSNFLGAyDSIRTSYNTSrdAENRANKSATDIPSTVS 813
Cdd:NF041483 633 QEAERLRTeAAADASAARA--EGENVAVRLRSEAAA-EAERLKSEAQESA-DRVRAEAAAA--AERVGTEAAEALAAAQE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQlldmKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDH 893
Cdd:NF041483 707 EAARRRREAEETLGSARAEADQERERAREQSEELLASAR----KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRD 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 894 SNNDLRDLIKQirEFLMLEGAdpdsIEAVANRVlelsipaspkqiRHLADEIKDRVKSlsnvDAILEQTqndvRKAEqll 973
Cdd:NF041483 783 SVAGLQEQAEE--EIAGLRSA----AEHAAERT------------RTEAQEEADRVRS----DAYAERE----RASE--- 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 974 lDAKKARNKAEGVKDTTVS-----VKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTAQERDldNAMDRLGD 1048
Cdd:NF041483 834 -DANRLRREAQEETEAAKAlaertVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADARE--DANRIRSD 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1049 LGRQIEAL---KTKRANNSLDAARAE------ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAER 1119
Cdd:NF041483 911 AAAQADRLigeATSEAERLTAEARAEaerlrdEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAER 990
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1120 LRDEAKELLKDAHDKLQRL-----EELEKDYDENQQVLEGK----AKQLDGLEDKMKAILSAINKKIQiynTSGLRLGND 1190
Cdd:NF041483 991 IRTEAERVKAEAAAEAERLrtearEEADRTLDEARKDANKRrseaAEQADTLITEAAAEADQLTAKAQ---EEALRTTTE 1067
|
....*
gi 2516233906 1191 SEMSA 1195
Cdd:NF041483 1068 AEAQA 1072
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-1126 |
1.17e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 658 LATRTKALTDRAKElQTTGLTRAFERKFNDLEGKLAQAReivnarnATAEAVtilmgmieelrgqIGETTETlnqlegdl 737
Cdd:NF041483 241 LRSSTAAESDQARR-QAAELSRAAEQRMQEAEEALREAR-------AEAEKV-------------VAEAKEA-------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 738 TAVQDSNYEASNALSTleREAKElnlnsdQLNRQLeilknsnflgaydsirtsyntsrdaeNRANKSATDIPSTVSQS-A 816
Cdd:NF041483 292 AAKQLASAESANEQRT--RTAKE------EIARLV--------------------------GEATKEAEALKAEAEQAlA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 817 DTRKKTERLMSEkrddfnrknAANK-RTLTDLNAKAQLLDMKKINEKVAdakTKAQE-AKNKAQAALEKASDAKKKVDHS 894
Cdd:NF041483 338 DARAEAEKLVAE---------AAEKaRTVAAEDTAAQLAKAARTAEEVL---TKASEdAKATTRAAAEEAERIRREAEAE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 895 NNDLRDLIKQIREflMLEGADPDSIEAVANRVLELSIPA-----SPKQIRHLADEIKDRVKSLSNVDAIlEQTQNDVRKA 969
Cdd:NF041483 406 ADRLRGEAADQAE--QLKGAAKDDTKEYRAKTVELQEEArrlrgEAEQLRAEAVAEGERIRGEARREAV-QQIEEAARTA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 970 EQLLldaKKARNKAEGVKDTTvsvkqalndagkaqaaaekaiekarndigltqnrlaqiqseTTAQERDLDNAMDRLGDL 1049
Cdd:NF041483 483 EELL---TKAKADADELRSTA-----------------------------------------TAESERVRTEAIERATTL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1050 GRQI-EALKTKRANNSLDAARAEETATMARDKANEAKEIL---------------DGELSDKYRTVQGLMDNKVKTMQEA 1113
Cdd:NF041483 519 RRQAeETLERTRAEAERLRAEAEEQAEEVRAAAERAARELreeteraiaarqaeaAEELTRLHTEAEERLTAAEEALADA 598
|
490
....*....|...
gi 2516233906 1114 KQKAERLRDEAKE 1126
Cdd:NF041483 599 RAEAERIRREAAE 611
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
783-1159 |
1.24e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 783 AYDSIRTSYNTS---RDAENRANKSATDIPSTVSqsaDTRKKTERLMSEKRDDFNR------KNAANKRTLTD--LNAKA 851
Cdd:NF041483 64 AYDGADIGYQAEqllRNAQIQADQLRADAERELR---DARAQTQRILQEHAEHQARlqaelhTEAVQRRQQLDqeLAERR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 852 QLLDmKKINEKVADAKTKAQEAKNKAQAALEKA-SDAKKKVDHSNNDLRDLIKQIREFLmleGADPDSIEAVANRVL--- 927
Cdd:NF041483 141 QTVE-SHVNENVAWAEQLRARTESQARRLLDESrAEAEQALAAARAEAERLAEEARQRL---GSEAESARAEAEAILrra 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 928 ----ELSIPASPKQIRHLADEIKD-RVKSLSNVDAILEQTQNDVRKAEQLLLDA----KKARNKAEGVkdttvsVKQALN 998
Cdd:NF041483 217 rkdaERLLNAASTQAQEATDHAEQlRSSTAAESDQARRQAAELSRAAEQRMQEAeealREARAEAEKV------VAEAKE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 999 DAGKaqaaaekaiekarndigltqnRLAQIQSETTAQERDLDNAMDRL-GDLGRQIEALKTKrANNSLDAARAE------ 1071
Cdd:NF041483 291 AAAK---------------------QLASAESANEQRTRTAKEEIARLvGEATKEAEALKAE-AEQALADARAEaeklva 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1072 ETATMARDKANE------------AKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEakellkdAHDKLQRLE 1139
Cdd:NF041483 349 EAAEKARTVAAEdtaaqlakaartAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGE-------AADQAEQLK 421
|
410 420 430
....*....|....*....|....*....|.
gi 2516233906 1140 ELEKD-----------YDENQQVLEGKAKQL 1159
Cdd:NF041483 422 GAAKDdtkeyraktveLQEEARRLRGEAEQL 452
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
936-1197 |
1.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 936 KQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKAR 1015
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1016 NDIGLTQNRL----AQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAAR---------AEETATMARDKAN 1082
Cdd:COG4372 125 QDLEQQRKQLeaqiAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEqaldellkeANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1083 EAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGL 1162
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260 270
....*....|....*....|....*....|....*
gi 2516233906 1163 EDKMKAILSAINKKIQIYNTSGLRLGNDSEMSAQE 1197
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
841-1198 |
1.52e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.00 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 841 KRTLTDLNAKAQLL--DMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKV-----------DHSNNDLRDLIKQIRE 907
Cdd:pfam06160 85 KKALDEIEELLDDIeeDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLlanrfsygpaiDELEKQLAEIEEEFSQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 908 F--LMLEGadpDSIEAvaNRVLElsipaspkQIRHLADEIKDRVKSlsnVDAILEQTQNDVrkAEQLL-LDAKKARNKAE 984
Cdd:pfam06160 165 FeeLTESG---DYLEA--REVLE--------KLEEETDALEELMED---IPPLYEELKTEL--PDQLEeLKEGYREMEEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 985 GVKDTTVSVKQALNDAgkaqaaaekaiekaRNDIGLTQNRLAQIqsettaqerDLDNAMDRLGDLGRQIEALKtkranns 1064
Cdd:pfam06160 227 GYALEHLNVDKEIQQL--------------EEQLEENLALLENL---------ELDEAEEALEEIEERIDQLY------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1065 ldaaraeetatmardkaneakEILDGELsDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAkELLKD----AHDKLQR--- 1137
Cdd:pfam06160 277 ---------------------DLLEKEV-DAKKYVEKNLPEIEDYLEHAEEQNKELKEEL-ERVQQsytlNENELERvrg 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1138 ----LEELEKDYDENQQVLEGKAKQLDGLEDKMKAI---LSAINKKIQIYNTS--GLRlgnDSEMSAQEQ 1198
Cdd:pfam06160 334 lekqLEELEKRYDEIVERLEEKEVAYSELQEELEEIleqLEEIEEEQEEFKESlqSLR---KDELEAREK 400
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1033-1175 |
1.74e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.05 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1033 TAQERDLDNAMDRLGDLGRQIEALKTKrANNSLDAARAEETATMARDKA-----NEAKEILDGELSDKYRT-VQGLMDNK 1106
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDK-AAKVVDKLTDFENQTEKDQTAletleKALKDLLTDEGGAIARKeIKDLQKEL 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1107 VKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELekdydenQQVLEGKAKQLDGLEDKMKAILSAINK 1175
Cdd:cd22656 189 EKLNEEYAAKLKAKIDELKALIADDEAKLAAALRL-------IADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
681-1180 |
2.48e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.59 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 681 FERKFNDLEGKLAQARE------------IVNAR---NATAEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVQDSN- 744
Cdd:PTZ00440 1082 LEEKVEALLKKIDENKNklieiknkshehVVNADkekNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNe 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 745 ----YEA------------SNALSTLEREAKEL---NLNSDQLN---RQLEILKNSNFLGAYDSIRTSYNTSRDAENRAN 802
Cdd:PTZ00440 1162 ieieYERilidhiveqinnEAKKSKTIMEEIESykkDIDQVKKNmskERNDHLTTFEYNAYYDKATASYENIEELTTEAK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 803 ksatdipsTVSQSADTRKKTERLMSEKRD---------DFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEA 873
Cdd:PTZ00440 1242 --------GLKGEANRSTNVDELKEIKLQvfsylqqviKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAEEF 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 874 KNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLmlegaDPDSIEAVANRVlelsipaspKQIRHLADEIKDRVKS-L 952
Cdd:PTZ00440 1314 SNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSL-----EDKQIDDEIKKI---------EQIKEEISNKRKEINKyL 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 953 SNVDAILEQTQNDVRKAEQL-----LLDAKKARNKAEG-------VKDTTVSVKQALNDAGKAQAAAEKAIEK---ARND 1017
Cdd:PTZ00440 1380 SNIKSNKEKCDLHVRNASRGkdkidFLNKHEAIEPSNSkevniikITDNINKCKQYSNEAMETENKADENNDSiikYEKE 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1018 IGLTQNRLAQIQSETTAQERdLDNAMDRLGDLGRQIEALKTKRANNSldaaraeETATMARDKAN--EAKEILDGELSDK 1095
Cdd:PTZ00440 1460 ITNILNNSSILGKKTKLEKK-KKEATNIMDDINGEHSIIKTKLTKSS-------EKLNQLNEQPNikREGDVLNNDKSTI 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1096 -YRTVQ---GLMDNKVKTMQEAKQKAERLRDEAKELLKD--------AHDKLQRLEELEKDYDEN-------QQVLEGKA 1156
Cdd:PTZ00440 1532 aYETIQynlGRVKHNLLNILNIKDEIETILNKAQDLMRDiskiskivENKNLENLNDKEADYVKYldnilkeKQLMEAEY 1611
|
570 580
....*....|....*....|....
gi 2516233906 1157 KQLDGLEDKMKAILSAINKKIQIY 1180
Cdd:PTZ00440 1612 KKLNEIYSDVDNIEKELKKHKKNY 1635
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1020-1210 |
2.54e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1020 LTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATmARDKANEAKEILDGELSDKYRTV 1099
Cdd:TIGR02169 284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1100 QGLMDNKVKTMQEAKQKAERLRDEAKElLKDAHDKLQR-LEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQ 1178
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKD-YREKLEKLKReINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190
....*....|....*....|....*....|..
gi 2516233906 1179 IYNTSGLrlgndsEMSAQEQQPSTLTSNAAKI 1210
Cdd:TIGR02169 442 EKEDKAL------EIKKQEWKLEQLAADLSKY 467
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
656-1220 |
3.25e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.21 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 656 QDLATRTKALTDRAKELQTTGLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEG 735
Cdd:PTZ00440 612 EKFINEKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIK 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 736 DLTAvqdsnyEASNaLSTLEREAKELNLNsdqlNRQLEILKNSN-FLGAYDSIRTSYNTSRDAENRANKSATDIPSTVSQ 814
Cdd:PTZ00440 692 NLKK------ELQN-LLSLKENIIKKQLN----NIEQDISNSLNqYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNE 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 815 SADTRKKTERLMSEKRDDFNRKNAaNKRTLtdLNAKAQLL-DMKKINEKVADAKTKaqeaKNKAQAALEKASDAKKKVDH 893
Cdd:PTZ00440 761 FILHLYENDKDLPDGKNTYEEFLQ-YKDTI--LNKENKISnDINILKENKKNNQDL----LNSYNILIQKLEAHTEKNDE 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 894 SNNDLRDLIKQIREFLMLEGADPDSIEAvaNRVLELSIpaspKQIRHLADEIkDRVKSLSNVdaiLEQTQNDVRKAEQLL 973
Cdd:PTZ00440 834 ELKQLLQKFPTEDENLNLKELEKEFNEN--NQIVDNII----KDIENMNKNI-NIIKTLNIA---INRSNSNKQLVEHLL 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 974 ldakkaRNKAEGVKDTTVSVKQALNDAGKAQAAaekaiekarndiglTQNRLAQIQSETTAQERDLDNAmdRLGDLGRQI 1053
Cdd:PTZ00440 904 ------NNKIDLKNKLEQHMKIINTDNIIQKNE--------------KLNLLNNLNKEKEKIEKQLSDT--KINNLKMQI 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1054 EAL-----KTKRANNSLDAARAEETatmarDKANEAKEILDGE---LSDKYRTVQGLMDNKVKT------------MQEA 1113
Cdd:PTZ00440 962 EKTleyydKSKENINGNDGTHLEKL-----DKEKDEWEHFKSEidkLNVNYNILNKKIDDLIKKqhddiielidklIKEK 1036
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1114 KQKAERLRDEAKELLKDAHDKLQRL---EELEKDYDENQQvlegkaKQLDGLEDKMKAILSAINK-KIQIYNTSGLRLGN 1189
Cdd:PTZ00440 1037 GKEIEEKVDQYISLLEKMKTKLSSFhfnIDIKKYKNPKIK------EEIKLLEEKVEALLKKIDEnKNKLIEIKNKSHEH 1110
|
570 580 590
....*....|....*....|....*....|....*
gi 2516233906 1190 ----DSEMSAQEQQPSTLTSNAAKIAGPGRKRHNS 1220
Cdd:PTZ00440 1111 vvnaDKEKNKQTEHYNKKKKSLEKIYKQMEKTLKE 1145
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1078-1199 |
3.76e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1078 RDKANEAKEIL--DGELSDKYrtvqglmdnkvKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLEGK 1155
Cdd:cd16269 177 QSKEAEAEAILqaDQALTEKE-----------KEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK 245
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2516233906 1156 AKQLdgLEDKMKAILSAINKKIQIyNTSGLRLGNDSEMSAQEQQ 1199
Cdd:cd16269 246 MEEE--RENLLKEQERALESKLKE-QEALLEEGFKEQAELLQEE 286
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
670-909 |
3.87e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.56 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 670 KELQTTGLTRAFERKFNDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQLEGDLTAVqdsnyeasn 749
Cdd:pfam06008 45 LEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFAL--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 750 ALSTLEREAKElnlnsdqLNRQLEILKNSNFlgaydsirtsynTSRDAENRANKsatdipstvsqsadtrKKTERLMSEK 829
Cdd:pfam06008 116 PSSDLSRMLAE-------AQRMLGEIRSRDF------------GTQLQNAEAEL----------------KAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 830 RDDFNRKNAANKRTLTDLNakaQLLDmkKINEKVADAKTKAQEAKNKA----------QAALEKASDAKKKVDHSNNDLR 899
Cdd:pfam06008 161 QTWFQSPQEENKALANALR---DSLA--EYEAKLSDLRELLREAAAKTrdanrlnlanQANLREFQRKKEEVSEQKNQLE 235
|
250
....*....|
gi 2516233906 900 DLIKQIREFL 909
Cdd:pfam06008 236 ETLKTARDSL 245
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1077-1197 |
3.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1077 ARDKANEAKEILDGELSDKYRTVQGLMDNKVktmQEAKQKAERLRDEAKELLKDAHDKLQRLEEL----EKDYDENQQVL 1152
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFEKELRERRNELQKLEKRllqkEENLDRKLELL 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2516233906 1153 EGKAKQLDGLEDKMKAILSAINKKIQ----IYNTSGLRLGNDSEMSAQE 1197
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEeleeLIEEQLQELERISGLTAEE 154
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
847-1170 |
4.52e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 847 LNAKAQ--LLDM----KKINEKVADAKTKAQEAKNKAQAALEKASDAKKKvdhsnndlRDLIK-QIREflmLEGADPDSI 919
Cdd:COG0497 138 LDPDAQreLLDAfaglEELLEEYREAYRAWRALKKELEELRADEAERARE--------LDLLRfQLEE---LEAAALQPG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 920 EAvanrvlelsipaspkqirhlaDEIKDRVKSLSNVDAILEQTQNdvrkAEQLLLDAkkarnkaegvkdtTVSVKQALND 999
Cdd:COG0497 207 EE---------------------EELEEERRRLSNAEKLREALQE----ALEALSGG-------------EGGALDLLGQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1000 AGKAqaaaekaiekarndigLtqNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALktkRANNSLDAARAEETatmard 1079
Cdd:COG0497 249 ALRA----------------L--ERLAEYDPSLAELAERLESALIELEEAASELRRY---LDSLEFDPERLEEV------ 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1080 kanEAK--EILDgeLSDKYRtvqglmdnkvKTMQEAKQKAERLRDEAKELlkDAHDklQRLEELEKDYDENQQVLEGKAK 1157
Cdd:COG0497 302 ---EERlaLLRR--LARKYG----------VTVEELLAYAEELRAELAEL--ENSD--ERLEELEAELAEAEAELLEAAE 362
|
330 340
....*....|....*....|.
gi 2516233906 1158 QL--------DGLEDKMKAIL 1170
Cdd:COG0497 363 KLsaarkkaaKKLEKAVTAEL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1144 |
5.05e-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: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 861 EKVADAKTKAQEAKNKAQAALEKASDAKKKVDhSNNDLRDLIKQIREFLMLEgadpdsieavanrvleLSIPASPKQIRH 940
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDE----------------IDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 941 LADEIKDRVKSLSNVDAILEQtqndVRKAEQLLLDAKKARNKAEGvkdttvsvkqalndagkaqaaaekaiekarnDIGL 1020
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQ----LEELEAELEELEEELDELKG-------------------------------EIGR 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1021 TQNRLAQIQSEttaqerdLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSDKYRTVq 1100
Cdd:COG4913 718 LEKELEQAEEE-------LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL- 789
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2516233906 1101 glmdnkVKTMQEAKQkaeRLRDEAKEL---LKDAHDKLQRLEELEKD 1144
Cdd:COG4913 790 ------ERAMRAFNR---EWPAETADLdadLESLPEYLALLDRLEED 827
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
938-1153 |
5.81e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 938 IRHLADEIKDRVKslsnvdaILEQTqndVRKAEQLLLDAKK--ARNKAEgVKDTTVSVKQALNDAGKAQAAAEKAIEKAR 1015
Cdd:COG1842 14 INALLDKAEDPEK-------MLDQA---IRDMEEDLVEARQalAQVIAN-QKRLERQLEELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1016 NDI---GLTqnRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKrannsLDAARAEETATMARDKANEAKEildgEL 1092
Cdd:COG1842 83 EDLareALE--RKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESK-----LEELKAKKDTLKARAKAAKAQE----KV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2516233906 1093 SDKYRTVQGlmDNKVKTMQEAKQKAERLRDEAK---ELlkDAHDKLQ-RLEELEKDyDENQQVLE 1153
Cdd:COG1842 152 NEALSGIDS--DDATSALERMEEKIEEMEARAEaaaEL--AAGDSLDdELAELEAD-SEVEDELA 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
654-1174 |
5.83e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 654 IVQDLATRTKALTDRAKELQTTGLTRAFErkFNDLEGKLAQAREIVNARNATAEavtilmgmieELRGQIGETTETLNQL 733
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSA--FRDLQGQLAHAKKQQELQQRYAE----------LCAAAITCTAQCEKLE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 EGDLTAVQDSNYEASNALSTLE----REAKELNLNSDQLNRQLE---ILKNSNF---LGAYDSIRTSYNTSR--DAENRA 801
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEqihlQETRKKAVVLARLLELQEepcPLCGSCIhpnPARQDIDNPGPLTRRmqRGEQTY 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 802 NKSATDIPSTVSQSADTRKKTERL---MSEKRDDFNRKNAANKRTLTDLNAKAQLLD-MKKINEKVADAKTKAQEAKNKA 877
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLkeqMQEIQQSFSILTQCDNRSKEDIPNLQNITVrLQDLTEKLSEAEDMLACEQHAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 878 QAALEKASDAKKKVDHSNNDLRDLIKqirEFLMLEGA------DPDSIEAVANRVLELSipaSPKQIRHLADEIKDRVKS 951
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELAL---KLTALHALqltltqERVREHALSIRVLPKE---LLASRQLALQKMQSEKEQ 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 952 LSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAgkAQAAAEKAIEKARNDIGLTQNRLAQIQSE 1031
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA--LNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1032 TTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETatmaRDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQ 1111
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE----IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1112 EAKQkaerlrdeakELLKDAhDKLQRLEELEKDYDENQQvLEGKAKQLDGL-----EDKMKAILSAIN 1174
Cdd:TIGR00618 846 EITH----------QLLKYE-ECSKQLAQLTQEQAKIIQ-LSDKLNGINQIkiqfdGDALIKFLHEIT 901
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
938-1153 |
6.18e-04 |
|
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: 42.74 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 938 IRHLADEIKDRVKSLSNVDAILEQTQndvRKAEQLLLDAKKARNKAegvkdttvsvKQALNdagkaqaaaekaiekaRND 1017
Cdd:pfam04012 31 IRDMQSELVKARQALAQTIARQKQLE---RRLEQQTEQAKKLEEKA----------QAALT----------------KGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1018 IGLTQNRLAQIQS---ETTAQERDLDNAMDRLGDLGRQIEALKTKrannsLDAARAEETATMARDKANEAKEILDgELSD 1094
Cdd:pfam04012 82 EELAREALAEKKSlekQAEALETQLAQQRSAVEQLRKQLAALETK-----IQQLKAKKNLLKARLKAAKAQEAVQ-TSLG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1095 KYRTvQGLMDnKVKTMQEaKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLE 1153
Cdd:pfam04012 156 SLST-SSATD-SFERIEE-KIEEREARADAAAELASAVDLDAKLEQAGIQMEVSEDVLA 211
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1070-1175 |
6.51e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1070 AEETATMARDKA------NEAKEILDgELSDKYRTVQ---GLMDNKVKTMQEAKQK-AERLRDEAKELLKDAHDKLQRLE 1139
Cdd:smart00787 150 DENLEGLKEDYKllmkelELLNSIKP-KLRDRKDALEeelRQLKQLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110
....*....|....*....|....*....|....*.
gi 2516233906 1140 ELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINK 1175
Cdd:smart00787 229 ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
657-883 |
7.90e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 657 DLATRTKALTDRAKELqttgltRAFERKFNDlegklaQAREIVNARNATAEAVTILMGMIEELRGQIGEttetLNQLEGD 736
Cdd:COG1340 47 ELNAQVKELREEAQEL------REKRDELNE------KVKELKEERDELNEKLNELREELDELRKELAE----LNKAGGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 737 LTA----VQDSNYEASNALSTLEREaKELNLNSDQLNRQLEILKNSN-FLGAYDSIRTSYNTSRDAENRANKSATDIpST 811
Cdd:COG1340 111 IDKlrkeIERLEWRQQTEVLSPEEE-KELVEKIKELEKELEKAKKALeKNEKLKELRAELKELRKEAEEIHKKIKEL-AE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 812 VSQSA-----DTRKKTERLMsEKRDDFNRK-----NAANK------RTLTDLNAKAQLLD-MKKINEKVADAKTKAqEAK 874
Cdd:COG1340 189 EAQELheemiELYKEADELR-KEADELHKEiveaqEKADElheeiiELQKELRELRKELKkLRKKQRALKREKEKE-ELE 266
|
....*....
gi 2516233906 875 NKAQAALEK 883
Cdd:COG1340 267 EKAEEIFEK 275
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
658-1118 |
9.59e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 658 LATRTKALTDRAKELQTTgLTRAfERKFNDL-EGKLAQAREIVNARN---ATAEAVTILMGMIEELRGQIGETTETLNQL 733
Cdd:pfam10174 343 LQTEVDALRLRLEEKESF-LNKK-TKQLQDLtEEKSTLAGEIRDLKDmldVKERKINVLQKKIENLQEQLRDKDKQLAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 EGDLTAVQDSNYEASNALSTLE------------------REAKELNLNSDQLNRQLEILKNSnfLGAYDSIRTSYNTS- 794
Cdd:pfam10174 421 KERVKSLQTDSSNTDTALTTLEealsekeriierlkeqreREDRERLEELESLKKENKDLKEK--VSALQPELTEKESSl 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 795 RDAENRANKSATDIPSTVSQSadtrKKTERLMSEKRDDFNR---------KNAANKRTLTDLNAKAQLLDmkkinekvAD 865
Cdd:pfam10174 499 IDLKEHASSLASSGLKKDSKL----KSLEIAVEQKKEECSKlenqlkkahNAEEAVRTNPEINDRIRLLE--------QE 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 866 AKTKAQEAkNKAQAALEKASDAKKKVDHSNNDlRDliKQIREFlmlegadpdsiEAVANRvlelsipaspkqirhladEI 945
Cdd:pfam10174 567 VARYKEES-GKAQAEVERLLGILREVENEKND-KD--KKIAEL-----------ESLTLR------------------QM 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 946 KDRVKSLSNVDAIleqTQNDVRKAEQLLLDAKKaRNKAEGVKDTTVSVKQALNDAGKAqaaaekaiekaRNDIGLTQNRL 1025
Cdd:pfam10174 614 KEQNKKVANIKHG---QQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKT-----------RQELDATKARL 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1026 AQIQSETTAQERDLDN-AMDRLGDLGrqiEALKTKRanNSLDAARAEETATMArdkaneakeILDGELSDKYRT---VQG 1101
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNlRAERRKQLE---EILEMKQ--EALLAAISEKDANIA---------LLELSSSKKKKTqeeVMA 744
|
490
....*....|....*..
gi 2516233906 1102 LMDNKVKTMQEAKQKAE 1118
Cdd:pfam10174 745 LKREKDRLVHQLKQQTQ 761
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
747-1060 |
9.59e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 747 ASNALSTLEREAKELNLNSDQLNRQLEIL-KNSNFLGAYDSIRTSyntSRDAE-----NRANKSATDIPSTVSQSADTRK 820
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERLrREREKAERYQALLKE---KREYEgyellKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 821 KTERLmSEKRDDFNRKNAANKRTLTDLNAKAQLL---DMKKINEKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNND 897
Cdd:TIGR02169 252 ELEKL-TEEISELEKRLEEIEQLLEELNKKIKDLgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 898 LRDLIKQIREF---LMLEGADPDSI-EAVANR-----VLELSIPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRK 968
Cdd:TIGR02169 331 IDKLLAEIEELereIEEERKRRDKLtEEYAELkeeleDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 969 ----AEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSEttaqerdLDNAMD 1044
Cdd:TIGR02169 411 lqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE-------YDRVEK 483
|
330
....*....|....*.
gi 2516233906 1045 RLGDLGRQIEALKTKR 1060
Cdd:TIGR02169 484 ELSKLQRELAEAEAQA 499
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
790-898 |
9.91e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 42.79 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 790 SYNTSRDAENrANKSATDIPSTVSQSADTRKKTERLMS---EKRDDFNRKNAANKRTLTDLNAKAQLLdmKKINEKVADA 866
Cdd:TIGR04320 232 NFNDSYIADG-NKFDKTPIPNPPNSLAALQAKLATAQAdlaAAQTALNTAQAALTSAQTAYAAAQAAL--ATAQKELANA 308
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2516233906 867 K-TKAQEAKN---KAQAALEKAS----DAKKKVDHSNNDL 898
Cdd:TIGR04320 309 QaQALQTAQNnlaTAQAALANAEarlaKAKEALANLNADL 348
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
732-1203 |
1.06e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 43.54 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 732 QLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQleilknsnflGAYDSI-------------------RTSYN 792
Cdd:COG5644 74 SFNASKSGKSNKDHKNLNNTKEISLNDSDDSVNSDKLENE----------GSVSSIdenelvdldtlldndqpekNESGN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 793 TSRDAENRANKSATDIPSTVSQSADTRkkterlmSEKRDDFNRKNAANKRTLTDLNAKAQLLDMKKINEkvADAKTKAQE 872
Cdd:COG5644 144 NDHATDKENLLESDASSSNDSESEESD-------SESEIESSDSDHDDENSDSKLDNLRNYIVSLKKDE--ADAESVLSS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 873 AKNKAQAALE-------KASDAKKKVDhsnndLRDLIKQIREFLMLEGADPdsieaVANRVLELSIPaspkqirhLADEI 945
Cdd:COG5644 215 DDNDSIEEIKydphetnKESGSSETID-----ITDLLDSIPMEQLKVSLKP-----LVSESSKLDAP--------LAKSI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 946 KDRVKSlsnvDAILEQTQNDV----------RKAEQLLLDAKKA----------RNKAEGVKDTTVSVKQALNDAGKAQA 1005
Cdd:COG5644 277 QDRLER----QAAYEQTKNDLekwkpivadnRKSDQLIFPMNETarpvpsnnglASSFEPRTESERKMHQALLDAGLENE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1006 AAEKAIEKarndigLTQNRLA-QIQSETTAQERDLDNAMDRLGDLGRQIEALKTK--RANNSLDAARAEETATMARDKAN 1082
Cdd:COG5644 353 SALKKQEE------LALNKLSvEEVAERTRQLRFMRELMFREERKAKRVAKIKSKtyRKIRKNRKEKEMALIPKSEDLEN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1083 EAKEILDGelsdKYRTVQGLMDNK--VKTMQEAKQKAERLRDEAKELLKDAHDKLQRLeeLEKDYDENQQVLEGKAKQLD 1160
Cdd:COG5644 427 EKSEEARA----LERMTQRHKNTSswTRKMLERASHGEGTREAVNEQIRKGDELMQRI--HGKEIMDGEDVSEFSDSDYD 500
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2516233906 1161 GlEDKMKAILSAINKKIQIYNTSGLRLGNDSEMSAQEQQPSTL 1203
Cdd:COG5644 501 T-NEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQMAASKISV 542
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
655-910 |
1.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 655 VQDLATRTKALTDRAKELQTTGLTraFERKFNDLEGKLA-QAREIVNARNATAEAVTILMGMIEELRGQIGETTETLNQL 733
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQT--LDMKIDHIQQQIKtYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 734 EGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSnflgayDSIRTSYNTSRDAENRANKSATDIPSTVS 813
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG------GVCPTCTQQISEGPDRITKIKDKLKELQH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 814 QSADTRKKTERLmSEKRDDFNRknaaNKRTLTDLNAkaqlldmkKINEKVADAKTKAQEAKnKAQAALEKASDA----KK 889
Cdd:PHA02562 314 SLEKLDTAIDEL-EEIMDEFNE----QSKKLLELKN--------KISTNKQSLITLVDKAK-KVKAAIEELQAEfvdnAE 379
|
250 260
....*....|....*....|.
gi 2516233906 890 KVDHSNNDLRDLIKQIREFLM 910
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSELVK 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1021-1199 |
1.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1021 TQNRLAQiqsettAQERdLDNAMDRLGDLGRQIEALKT---------------------------KRANNSLDAARAE-E 1072
Cdd:COG1196 177 AERKLEA------TEEN-LERLEDILGELERQLEPLERqaekaeryrelkeelkeleaellllklRELEAELEELEAElE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1073 TATMARDKANEAKEILDGELsDKYRTVQGLMDNKVKTMQ----EAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDEN 1148
Cdd:COG1196 250 ELEAELEELEAELAELEAEL-EELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 1149 QQVLEGKAKQLDGLEDKMKAILSAINKKIQIYNTSGLRLGNDSEMSAQEQQ 1199
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1082-1183 |
1.57e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1082 NEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKA----ERLRDEAKELLKDAHDKLQRLEELEkdydENQQVLEGKAK 1157
Cdd:pfam10168 538 SRATQVFREEYLKKHDLAREEIQKRVKLLKLQKEQQlqelQSLEEERKSLSERAEKLAEKYEEIK----DKQEKLMRRCK 613
|
90 100 110
....*....|....*....|....*....|....*..
gi 2516233906 1158 QLDGL-----------EDKMKAILSAINKKIQIYNTS 1183
Cdd:pfam10168 614 KVLQRlnsqlpvlsdaEREMKKELETINEQLKHLANA 650
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
796-1153 |
1.63e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 42.69 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 796 DAENRANKSATDIPSTVSQSADTRKKterlmsEKRDDFNRKNAANKRTLTDLNAKAQLLDMKKINEKVADAKTKAQEAKN 875
Cdd:COG5271 539 ETEGEENAPGSDQDADETDEPEATAE------EDEPDEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADD 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 876 -KAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAVANRVLELSIPASPKQIRHLADEIKDRVKSLSN 954
Cdd:COG5271 613 dEADADADGAADEEETEEEAAEDEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEAS 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 955 VDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGLTQNRLAQIQSETTA 1034
Cdd:COG5271 693 DDEEETEEADEDAETASEEADAEEADTEADGTAEEAEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEA 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1035 QERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGELSDKyrTVQGLMDNKVKTMQEAK 1114
Cdd:COG5271 773 LEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADE--ALEDIEAGIAEDDEEDD 850
|
330 340 350
....*....|....*....|....*....|....*....
gi 2516233906 1115 QKAERLRDEAKELLKDAHDKLQRLEELEKDYDENQQVLE 1153
Cdd:COG5271 851 DAAAAKDVDADLDLDADLAADEHEAEEAQEAETDADADA 889
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
913-1193 |
1.71e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 913 GADPDSIEAVANRVLELSipasPKQIRHLADEI------------------KDRVKSLSNV------D-----------A 957
Cdd:COG2268 100 NSDPEDIANAAERFLGRD----PEEIEELAEEKlegalravaaqmtveelnEDREKFAEKVqevagtDlaknglelesvA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 958 I--LEQTQN--D---VRKAEQLLLDAKKARNKAEgvKDTTVSVKQALNDAGKAQAAAEKAIEKARndIGLTQNRLAQIQS 1030
Cdd:COG2268 176 ItdLEDENNylDalgRRKIAEIIRDARIAEAEAE--RETEIAIAQANREAEEAELEQEREIETAR--IAEAEAELAKKKA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1031 ETTAQERDLDNAMDRLGDLGRQIEALKTKRAnnsLDAARAEETATMARDKANEAKEILDGELS-----DKYRTVqglmdn 1105
Cdd:COG2268 252 EERREAETARAEAEAAYEIAEANAEREVQRQ---LEIAEREREIELQEKEAEREEAELEADVRkpaeaEKQAAE------ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1106 kvktmQEAKQKAERLRDEAKellKDAhDKLQRLEELEKDYDENqQVLEGKAKQLDGLedkMKAILSAINK--KIQIYNTS 1183
Cdd:COG2268 323 -----AEAEAEAEAIRAKGL---AEA-EGKRALAEAWNKLGDA-AILLMLIEKLPEI---AEAAAKPLEKidKITIIDGG 389
|
330
....*....|
gi 2516233906 1184 GLRLGNDSEM 1193
Cdd:COG2268 390 NGGNGAGSAV 399
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
1071-1153 |
2.24e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1071 EETATMARDKANEAKEildgELSDKYRTVQGLMDNKVKtmqEAKQKAERLRDEAKELLKDAHDKLQR-LEELEKDYDENQ 1149
Cdd:COG4980 30 KETRKKLKDKADDLKD----KAEDLKDELKEKASELSE---EAKEKLDELIEEIKEKIEELKEEVEPkIEELKEEAEKLQ 102
|
....
gi 2516233906 1150 QVLE 1153
Cdd:COG4980 103 KEVE 106
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
650-947 |
2.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 650 DWDRIVQDLATRTKALTDRAKELQttgltRAFERKFNDLEgkLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTET 729
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQ-----RLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAE 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 730 LNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILKNSNFLGAYDSIrtsyntsrDAENRANKSATDIP 809
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA--------LGDAVERELRENLE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 810 STVSQSADTRKKTERLMSEKRDDFNRKNAANKRTL-TDLNAKAQLLDM-KKI-NEKVADAKTKAQEAKNKA--------Q 878
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAFNREWPAETADLdADLESLPEYLALlDRLeEDGLPEYEERFKELLNENsiefvadlL 852
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2516233906 879 AALEKA-SDAKKKVDHSNNDLRDLikqirEFlmleGADpdsieavanRVLELSI-PASPKQIRHLADEIKD 947
Cdd:COG4913 853 SKLRRAiREIKERIDPLNDSLKRI-----PF----GPG---------RYLRLEArPRPDPEVREFRQELRA 905
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1079-1178 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1079 DKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQ---KAERLRDEAKELLKDAHDKLQR-LEELEKDYDENQQVLEG 1154
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQlerRLEQQTEQAKKLEEKAQAALTKgNEELAREALAEKKSLEK 97
|
90 100 110
....*....|....*....|....*....|.
gi 2516233906 1155 KAKQLDGL-------EDKMKAILSAINKKIQ 1178
Cdd:pfam04012 98 QAEALETQlaqqrsaVEQLRKQLAALETKIQ 128
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
652-1140 |
2.46e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 652 DRIVQDLATRTKALTDR--------AKELQTTGLT----RAFERKFNDLEG-KLAQAREIVNarNATAEAVTI-LMgmie 717
Cdd:PRK04778 28 YKRIDELEERKQELENLpvndelekVKKLNLTGQSeekfEEWRQKWDEIVTnSLPDIEEQLF--EAEELNDKFrFR---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 718 ELRGQIGETTETLNQLEGDLTAVQDsnyeasnALSTLereakelnLNSDQLNRQleilknsnflgAYDSIRTSYNTSRD- 796
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILE-------ELQEL--------LESEEKNRE-----------EVEQLKDLYRELRKs 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 797 -AENRanksatdipstvSQSADTRKKTERLMSEKRDDFNRKNAAN--------KRTLTDLNAKAQLL--DMKKINEKVAD 865
Cdd:PRK04778 156 lLANR------------FSFGPALDELEKQLENLEEEFSQFVELTesgdyveaREILDQLEEELAALeqIMEEIPELLKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 866 AKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRdlIKQIREflmlegadpdSIEAVANRVLELSIPASPKQIRHLADEI 945
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE--IQDLKE----------QIDENLALLEELDLDEAEEKNEEIQERI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 946 KDRVKSLSN-VDAileqtQNDVRK-AEQLLLDAKKARNKAEGVKDTTVSVKQA--LNDagkaqaaaekaiekarNDIGLT 1021
Cdd:PRK04778 292 DQLYDILEReVKA-----RKYVEKnSDTLPDFLEHAKEQNKELKEEIDRVKQSytLNE----------------SELESV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1022 QNRLAQIQSETTAQERDLDN----------AMDRLGDLGRQIEALKTKRA--NNSLDAARAEETAtmARDKANEakeiLD 1089
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERiaeqeiayseLQEELEEILKQLEEIEKEQEklSEMLQGLRKDELE--AREKLER----YR 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2516233906 1090 GELSDKYRTVQ-----GL----MDNKVKTMQEAKQKAERLR------DEAKELLKDAHDKLQRLEE 1140
Cdd:PRK04778 425 NKLHEIKRYLEksnlpGLpedyLEMFFEVSDEIEALAEELEekpinmEAVNRLLEEATEDVETLEE 490
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
656-1175 |
2.52e-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: 42.34 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 656 QDLATRTKALTDraKELQTTGLTRAFERKFNDLEGKLAQAR-EIVNARNATAEAVTILMgMIEELRGQIGETT--ETLNQ 732
Cdd:TIGR00606 419 SKERLKQEQADE--IRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILE-LDQELRKAERELSkaEKNSL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 733 LEGDLTAVQDSNYEASNALSTLEREAKELnlnsDQLNRQLEILKNSNFLG-----AYDSIRTsyNTSRDAENRANKsATD 807
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKLDQEM----EQLNHHTTTRTQMEMLTkdkmdKDEQIRK--IKSRHSDELTSL-LGY 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 808 IPST--VSQSADTRKKTERLMSEKRDDFNRKNAANKRTLTDLNAKAQLLDMK--KINEKVADA-KTKAQEAK-NKAQAAL 881
Cdd:TIGR00606 569 FPNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQlsSYEDKLFDVcGSQDEESDlERLKEEI 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 882 EKASDAK----------------------------KKVDHSNNDLRDLIKQIREFLMLEgadPDSIEAVANRVLELS--- 930
Cdd:TIGR00606 649 EKSSKQRamlagatavysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLA---PDKLKSTESELKKKEkrr 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 931 ------IPASPKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLlDAKKARNKAEGVKDTTVSVKQALNDAGK-- 1002
Cdd:TIGR00606 726 demlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL-GTIMPEEESAKVCLTDVTIMERFQMELKdv 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1003 AQAAAEKAIEKARNDIGLT-----------QNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAE 1071
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTvqqvnqekqekQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ 884
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1072 ETATMARDKANEAKEiLDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKEllkdAHDKLQRLEELEKDYDENQQV 1151
Cdd:TIGR00606 885 QFEEQLVELSTEVQS-LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK----AQDKVNDIKEKVKNIHGYMKD 959
|
570 580
....*....|....*....|....
gi 2516233906 1152 LEGKAKqlDGLEDKMKAILSAINK 1175
Cdd:TIGR00606 960 IENKIQ--DGKDDYLKQKETELNT 981
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
848-1170 |
2.93e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 41.75 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 848 NAKAQL--LDMKKINEKVADAKTKAQEAKNkaqaALEKASDAKKKVDHSNNDLRDLIKQIREflmlegadpdsieavanr 925
Cdd:COG4477 266 EALELLeeLDLDEAEEELEEIEEEIDELYD----LLEKEVEAKKYVDKNQEELEEYLEHLKE------------------ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 926 vlelsipaspkQIRHLADEIkDRVKS---LSNVDAileqtqNDVRKAEQLLldakkarnkaegvkdttvsvkQALndagk 1002
Cdd:COG4477 324 -----------QNRELKEEI-DRVQQsyrLNENEL------EKVRNLEKQI---------------------EEL----- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1003 aqaaaekaiekarndigltQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRA--NNSLDAARAEEtatmardk 1080
Cdd:COG4477 360 -------------------EKRYDEIDERIEEEKVAYSELQEELEEIEEQLEEIEEEQEefSEKLKSLRKDE-------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1081 aNEAKEILdgelsDKYRtvqglmdnkvKTMQEAKQKAERLR-----DEAKELLKDAHDKLQRL-EELEK---DYDENQQV 1151
Cdd:COG4477 413 -LEAREKL-----DELK----------KKLREIKRRLEKSNlpglpEEYLEMFEEASDEIEELsEELNEvplNMDEVNRL 476
|
330
....*....|....*....
gi 2516233906 1152 LEGKAKQLDGLEDKMKAIL 1170
Cdd:COG4477 477 LEEAEEDIETLEEKTEELV 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
935-1092 |
3.53e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 935 PKQIRHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQalndagkaqaaaekaieka 1014
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE------------------- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2516233906 1015 rndigltqnrLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDGEL 1092
Cdd:COG1579 91 ----------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
788-1184 |
4.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 788 RTSYNTSRDAENRANKSAtdipstVSQSA-DTRKKTERLMSEKRDD------FNRKNAANKRTLTDLNAKAQLLDMKKIN 860
Cdd:PRK01156 88 RRGKGSRREAYIKKDGSI------IAEGFdDTTKYIEKNILGISKDvflnsiFVGQGEMDSLISGDPAQRKKILDEILEI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 861 EKVADAKTKAQEAKNKAQAALEKASDAKKKVDHSNNDLRDLIKQIREFLMLEGADPDSIEAvanrvLELSIPASPKQIRH 940
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIER-----LSIEYNNAMDDYNN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 941 LADEIKdRVKSLSNVDAILEQtqnDVRKAEQLLLDAKKARNKaegVKDTTVSVKQALNDAGKAQAAAEKAIEKARNDIGl 1020
Cdd:PRK01156 237 LKSALN-ELSSLEDMKNRYES---EIKTAESDLSMELEKNNY---YKELEERHMKIINDPVYKNRNYINDYFKYKNDIE- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1021 tqnRLAQIQSETTAQERDLDNAMDRLGDLGR-QIEALKTKRANNSLDaaraeetatmardkaneaKEILD-GELSDKYRT 1098
Cdd:PRK01156 309 ---NKKQILSNIDAEINKYHAIIKKLSVLQKdYNDYIKKKSRYDDLN------------------NQILElEGYEMDYNS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1099 VQGLMDNKVKTMQEAKQKAERLRDEAKELLK----DAHDKLQRLEELEKDYDEnqqvLEGKAKQLDGLEDKMKAILSAIN 1174
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQD----ISSKVSSLNQRIRALRENLDELS 443
|
410
....*....|
gi 2516233906 1175 KKIQIYNTSG 1184
Cdd:PRK01156 444 RNMEMLNGQS 453
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
851-1089 |
5.00e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 851 AQLLDMKKIN---EKVADAKTKAQ-EAKNKAQAALEKASDAKKKVDHSN------NDLRDLIKQIREFLMLEGADPDSIE 920
Cdd:PRK10929 20 ATAPDEKQITqelEQAKAAKTPAQaEIVEALQSALNWLEERKGSLERAKqyqqviDNFPKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 921 A-------------VANRVLELSIPASPKQIRhlADEIKDrvkSLSNvdaiLEQTQNDVRKAeqllLDAKKARNKAEGVK 987
Cdd:PRK10929 100 PnmstdaleqeilqVSSQLLEKSRQAQQEQDR--AREISD---SLSQ----LPQQQTEARRQ----LNEIERRLQTLGTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 988 DTTVSvkQALNDAGKAQAAAEKAIEkarNDIGLTQ----NR--LAQIQSEtTAQER--DLDNamdRLGDLGRQIEALKTK 1059
Cdd:PRK10929 167 NTPLA--QAQLTALQAESAALKALV---DELELAQlsanNRqeLARLRSE-LAKKRsqQLDA---YLQALRNQLNSQRQR 237
|
250 260 270
....*....|....*....|....*....|
gi 2516233906 1060 RANNSLdaaraEETATMARDKANEAKEILD 1089
Cdd:PRK10929 238 EAERAL-----ESTELLAEQSGDLPKSIVA 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1032-1211 |
5.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1032 TTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEETATMARDKANEAKEILDgELSDKYRTVQGLMDNKVKTMQ 1111
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1112 EAKQKAERLRDEAKELL------------------KDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAI 1173
Cdd:COG4942 94 ELRAELEAQKEELAELLralyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 2516233906 1174 NKKIQIYNT-SGLRLGNDSEMSAQEQQPSTLTSNAAKIA 1211
Cdd:COG4942 174 AELEALLAElEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
836-890 |
5.94e-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: 5.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2516233906 836 KNAANKRTLTDLNAKAQLldmKKINEKVADAKTKAQEAKNKAQAALEKASDAKKK 890
Cdd:TIGR02794 137 EAEAERKAKEEAAKQAEE---EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1038-1168 |
6.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1038 DLDNAMDRLGDLGRQIEALKtKRANNSLdaARAEETATMARDKANEAKEILD--GELSDKYRTVQGLMDN---KVKTMQE 1112
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRI-ERLEKFI--KRTENIEELIKEKEKELEEVLReiNEISSELPELREELEKlekEVKELEE 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1113 AKQKAERLRDEAKELLKDA---HDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKA 1168
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
656-1198 |
7.42e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 656 QDLATRTKALTDRAKELQTTGLTRAferkfnDLEGKLAQAREIVNARNATAEAVTILMGMIEELRgQIGETTETLNQLEG 735
Cdd:pfam10174 151 QTLGARDESIKKLLEMLQSKGLPKK------SGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENI-HLREELHRRNQLQP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 736 DLT---AVQDSNYEASNALSTLEREAKELNLnsdqlnrQLEILKNSNFLGAYDsirtsyntsRDAENR---ANKSATD-I 808
Cdd:pfam10174 224 DPAktkALQTVIEMKDTKISSLERNIRDLED-------EVQMLKTNGLLHTED---------REEEIKqmeVYKSHSKfM 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 809 PSTVSQ--SADTRKKTERL-MSEKRDDFNRKNAANKRTL----TDLNAKAQ--------------LLDMKkinEKVADAK 867
Cdd:pfam10174 288 KNKIDQlkQELSKKESELLaLQTKLETLTNQNSDCKQHIevlkESLTAKEQraailqtevdalrlRLEEK---ESFLNKK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 868 TKA----QEAKNKAQAALEKASDA-----------KKKVDHSNNDLRDLIKQIREF------LMLEGADPDSI-----EA 921
Cdd:pfam10174 365 TKQlqdlTEEKSTLAGEIRDLKDMldvkerkinvlQKKIENLQEQLRDKDKQLAGLkervksLQTDSSNTDTAlttleEA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 922 VANRvlELSIPASPKQI----RHLADEIKDRVKSLSNVDAILEQTQNDVRKAEQLLLDAKK--------ARNKAEGVKDT 989
Cdd:pfam10174 445 LSEK--ERIIERLKEQReredRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhasslassGLKKDSKLKSL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 990 TVSVKQALNDAGKAQAAAE---KAIEKARNDIGLTqNRLAQIQSETTaqeRDLDNAMDRLGDLGRQIEALK-TKRANNSL 1065
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKkahNAEEAVRTNPEIN-DRIRLLEQEVA---RYKEESGKAQAEVERLLGILReVENEKNDK 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1066 DAARAE---ETATMARDKANEAKEILDGELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEakelLKDAHDKL-QRLEEL 1141
Cdd:pfam10174 599 DKKIAElesLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEE----LMGALEKTrQELDAT 674
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2516233906 1142 EKDYDENQQVLEGKA-----------KQLDG-LEDKMKAILSAINKKIQiyNTSGLRLGNDSEMSAQEQ 1198
Cdd:pfam10174 675 KARLSSTQQSLAEKDghltnlraerrKQLEEiLEMKQEALLAAISEKDA--NIALLELSSSKKKKTQEE 741
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1111-1178 |
7.68e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 7.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2516233906 1111 QEAKQKAERLRDEAKELL----KDAHDKLQRLEELEKDYDENQQVLEGKAKQLDGLEDKMKAILSAINKKIQ 1178
Cdd:cd22656 106 ATDDEELEEAKKTIKALLddllKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIA 177
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1079-1169 |
7.69e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.22 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1079 DKANEAKEildgeLSDKYRT--VQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEKDYDE-NQQVLE-- 1153
Cdd:pfam06160 67 ELLFEAEE-----LNDKYRFkkAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElRKTLLAnr 141
|
90
....*....|....*....
gi 2516233906 1154 ---GKAkqLDGLEDKMKAI 1169
Cdd:pfam06160 142 fsyGPA--IDELEKQLAEI 158
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
667-775 |
7.87e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.05 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 667 DRAKELQTTGLTRAFERKFNDLEGK-LAQARE-----------IVNARNATAEavtilmgmIEELRGQIGETTETLNQLE 734
Cdd:pfam10473 1 DEKKQLHVLEKLKESERKADSLKDKvENLERElemseenqelaILEAENSKAE--------VETLKAEIEEMAQNLRDLE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2516233906 735 GDLTAVQDSNYEASNALSTLEREAKELN-LNSDqLNRQLEIL 775
Cdd:pfam10473 73 LDLVTLRSEKENLTKELQKKQERVSELEsLNSS-LENLLEEK 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1036-1199 |
8.15e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1036 ERDLDNA---MDRLGD----LGRQIEALKTKrannsldaarAEetatmardKANEAKEILDgELSDKYRTVQGLmdnkvk 1108
Cdd:TIGR02168 178 ERKLERTrenLDRLEDilneLERQLKSLERQ----------AE--------KAERYKELKA-ELRELELALLVL------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1109 TMQEAKQKAERLRDEAKElLKDAHDKLQR-LEELEKDYDENQ---QVLEGKAKQLDGLEDKMKAILSAINKKIQIYNTSG 1184
Cdd:TIGR02168 233 RLEELREELEELQEELKE-AEEELEELTAeLQELEEKLEELRlevSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
170
....*....|....*.
gi 2516233906 1185 LRLGNDSEM-SAQEQQ 1199
Cdd:TIGR02168 312 ANLERQLEElEAQLEE 327
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1018-1174 |
8.28e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1018 IGLTQNRLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDA-----------ARAEETATMARDKANEAKE 1086
Cdd:pfam06008 21 LENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAqqvnaesertlGHAKELAEAIKNLIDNIKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1087 ILD--------------GELSDKYRTVQGLMDN-KVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEElekdydENQQV 1151
Cdd:pfam06008 101 INEkvatlgendfalpsSDLSRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQE------ENKAL 174
|
170 180
....*....|....*....|...
gi 2516233906 1152 LEGKAKQLDGLEDKMKAILSAIN 1174
Cdd:pfam06008 175 ANALRDSLAEYEAKLSDLRELLR 197
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
785-1143 |
8.85e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.43 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 785 DSIRTSYNTSRDAENRANKSATDIPSTVSQSAdTRKKTERLmSEKRDDFNRKNAANKRTLTDLN----AKAQLLDMKKIN 860
Cdd:pfam13166 110 EKLDAAEANLQKLDKEKEKLEADFLDECWKKI-KRKKNSAL-SEALNGFKYEANFKSRLLREIEkdnfNAGVLLSDEDRK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 861 EKVADAKTKAQ------EAKNKAQAALEKASDAKKKVDHSNNDLRDLIK--QIREF----LMLEGADPDSI-----EAVA 923
Cdd:pfam13166 188 AALATVFSDNKpeiaplTFNVIDFDALEKAEILIQKVIGKSSAIEELIKnpDLADWveqgLELHKAHLDTCpfcgqPLPA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 924 NRVLELSipaspkqiRHLADEIKDRVKSLSN-VDAILEQTQN----------DVRKAEQLLLDAKKARNKAEGVKDTTVS 992
Cdd:pfam13166 268 ERKAALE--------AHFDDEFTEFQNRLQKlIEKVESAISSllaqlpavsdLASLLSAFELDVEDIESEAEVLNSQLDG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 993 VKQALNDagkaqaaaekaiekARNDIGltqnrlaqiqseTTAQERDLDNAMDRLGDLGRQIEALKTKRANNSLDAARAEE 1072
Cdd:pfam13166 340 LRRALEA--------------KRKDPF------------KSIELDSVDAKIESINDLVASINELIAKHNEITDNFEEEKN 393
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2516233906 1073 TA--TMARDKANEAKEILDgELSDKYRTVQGLMDNKVKTMQEAKQKAERLRDEAKELLKDAHDKLQRLEELEK 1143
Cdd:pfam13166 394 KAkkKLRLHLVEEFKSEID-EYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINK 465
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
934-1207 |
9.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 934 SPKQIRHLADEIKDRvKSLSNVDAI----LEQTQNDVRKAEQLLLDAKKARNKAEGVKDTTVSVKQALNDAGKAQAAAEK 1009
Cdd:PRK11281 37 TEADVQAQLDALNKQ-KLLEAEDKLvqqdLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1010 AIEKARNdigltqnrLAQIQSETTAQERDLDNAMDRLGDLGRQIEALKTK--RANNSLDAA--RAEETATMArDKANEAK 1085
Cdd:PRK11281 116 ETLSTLS--------LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQpeRAQAALYANsqRLQQIRNLL-KGGKVGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1086 EILDGELSDKYRTVQGLMDnkvktMQEAKQKaerlrdeaKELlkDAHDKLQRLEELEKDY-DENQQVLEgkaKQLDGLED 1164
Cdd:PRK11281 187 KALRPSQRVLLQAEQALLN-----AQNDLQR--------KSL--EGNTQLQDLLQKQRDYlTARIQRLE---HQLQLLQE 248
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2516233906 1165 kmkailsAINKKiqiyntsglRLgNDSEMSAQEQQPSTLTSNA 1207
Cdd:PRK11281 249 -------AINSK---------RL-TLSEKTVQEAQSQDEAARI 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
650-776 |
9.73e-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: 40.44 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 650 DWDRIVQDLATRTKALTdrakelqttgLTRAFERKfnDLEGKLAQAREIVNARNATAEAVTILMGMIEELRGQIGETTET 729
Cdd:TIGR02169 809 RIEARLREIEQKLNRLT----------LEKEYLEK--EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2516233906 730 LNQLEGDLTAVQDSNYEASNALSTLEREAKELNLNSDQLNRQLEILK 776
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1025-1140 |
9.78e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 37.53 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2516233906 1025 LAQIQSETTAQERDLDNAMDRLGDLGRQIEALKT--KRANNSLdaARAEETATMARDKAN-EAKEILdgelsdkyrtvqg 1101
Cdd:COG3599 29 LDEVAEDYERLIRENKELKEKLEELEEELEEYREleETLQKTL--VVAQETAEEVKENAEkEAELII------------- 93
|
90 100 110
....*....|....*....|....*....|....*....
gi 2516233906 1102 lmdnkvktmQEAKQKAERLRDEAKELLKDAHDKLQRLEE 1140
Cdd:COG3599 94 ---------KEAELEAEKIIEEAQEKARKIVREIEELKR 123
|
|
| |
