|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
1.35e-110 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 350.73 E-value: 1.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 35 CYPATGDLLIGRaqKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHetlnpdSHLIENVVTTFAPNRLKiWWQS 114
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 115 ENGV---ENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFpGISTGPMK--KVDDII 189
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 190 CDSRYSDIEPSTEGEVIFRAL--DPAFKIEDpYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIReKYYYAVYDMVV 267
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 167614504 268 RG 269
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
3.02e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 275.78 E-value: 3.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 29 GCAEGSCYPATGDLLIGRaqKLSVTSTCGLHKPEPYCI-VSHLQEDKKCFICNSQDPYHetlnpdSHLIENVVTTFAPNR 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 108 LKiWWQSEN---GVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSsDFGKTWGVYRYFAYDCEASFPGISTGPMKK 184
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 185 V--DDIICDSRYSDIEPSTEGEVIFRALDPAFKIED-PYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYA 261
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 167614504 262 VYDMVVRG 269
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1714-1786 |
2.45e-39 |
|
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: 140.69 E-value: 2.45e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1714 DARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTCL 1786
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTCL 73
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1224-1778 |
2.25e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1224 ERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKL--------IKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESL 1295
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkaeeKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1296 DNTVKELAEQLEFIKNSDiRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVmmERESQFKEKQEEQA 1375
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1376 RLLDEL----AGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKcggpgcgglvtVAHNAWQKAMDLDQ-D 1450
Cdd:PTZ00121 1405 KKADELkkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK-----------KAEEAKKKAEEAKKaD 1473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAE----VEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAV-- 1524
Cdd:PTZ00121 1474 EAKKKAEeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkk 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANEVLKMEMPSTPQQLQNLTEDireRVESLSQVEVILQHSAADIARAEMLLEEAKRA----SKSATDVKVTADMVKEALE 1600
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAKIKAEELKKAEE 1630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1601 E---AEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETlfnaSQRISELERNVEELKRKAAQNSGEAEYIEKVVY 1677
Cdd:PTZ00121 1631 EkkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1678 TVKQSAEDVKKT--LDGELDEKYKKVENLIAKKTEEsadaRRKAEmlqnEAKTLLAQANSKLQLLKDLERKYEDNQRYLE 1755
Cdd:PTZ00121 1707 LKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEED----KKKAE----EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
570 580
....*....|....*....|...
gi 167614504 1756 DKAQELARLEGEVRSLLKDISQK 1778
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
821-869 |
4.62e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.54 E-value: 4.62e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 821 CECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPSCQPCQC 869
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1778 |
2.55e-15 |
|
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: 79.81 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1559 VILQHSAADIARAEMLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAEL----------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1639 ETLFNASQRISELERNVEELKRK------AAQNSGEAEYIE------------KVVYTVKQSAEDVKKTLDgELDEKYKK 1700
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaellrALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1701 VENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1454-1769 |
2.62e-15 |
|
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: 82.04 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1454 ALAEVEQLSKMVSEAKLRADEAKQSAEDiLLKTNATKEKMDKSNEELRN-----LIKQIRNFLTQdsadldsIEAVANEV 1528
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLER-LRREREKAERYQALLKEKREyegyeLLKEKEALERQ-------KEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1529 LKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAADIAR---AEMLLEEAKRASKSAtDVKVTADMVKEALEEAEKA 1605
Cdd:TIGR02169 247 ASLE-----EELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeEEQLRVKEKIGELEA-EIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1606 QVAAEKA----------IKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQnsgEAEYIEKV 1675
Cdd:TIGR02169 321 EERLAKLeaeidkllaeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---YREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1676 vytvKQSAEDVKKTLDGELDEKYK----------KVENLIAKKTE---ESADARRKAEMLQNEAKTLLAQANSKLQLLKD 1742
Cdd:TIGR02169 398 ----KREINELKRELDRLQEELQRlseeladlnaAIAGIEAKINEleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340
....*....|....*....|....*..
gi 167614504 1743 LERKYEDNQRYLEDKAQELARLEGEVR 1769
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
773-818 |
3.67e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 70.80 E-value: 3.67e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGC 818
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
773-821 |
1.36e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 1.36e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGCKPC 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-819 |
3.11e-14 |
|
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: 68.53 E-value: 3.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 772 ACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGF--GPSGCK 819
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1187-1775 |
3.21e-13 |
|
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: 75.21 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1187 DVIIAELTNR------THRFLEKAKAlKISGVIGPYRETVDSVERKVSEIKDILAQSpaAEPLKNIGNLFEE--AEK--L 1256
Cdd:pfam01576 186 EAMISDLEERlkkeekGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKK--EEELQAALARLEEetAQKnnA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1257 IKDVTEMMAQVEVKLSDTTSQSNSTAK----------ELDSLQTEAE-SLDNTV--KELAEQLEfIKNSDIRGALDSITK 1323
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAARNKaekqrrdlgeELEALKTELEdTLDTTAaqQELRSKRE-QEVTELKKALEEETR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1324 YFQMSL-EAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEE-----QARLLDE-----LAGKLQSLDlsa 1392
Cdd:pfam01576 342 SHEAQLqEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqQAKQDSEhkrkkLEGQLQELQ--- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1393 aaemtcgtppgASCSETEcggpNCRTDEGERKcgGPGCGGLVTVAHN---AWQKAMDLDQDVLSA---LAEVEQLSKMVS 1466
Cdd:pfam01576 419 -----------ARLSESE----RQRAELAEKL--SKLQSELESVSSLlneAEGKNIKLSKDVSSLesqLQDTQELLQEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1467 EAKLRADEAKQSAEDillKTNATKEKMDKSNEELRNLIKQIRNfLTQDSADLDSieavanevlKME-MPSTPQQLqnltE 1545
Cdd:pfam01576 482 RQKLNLSTRLRQLED---ERNSLQEQLEEEEEAKRNVERQLST-LQAQLSDMKK---------KLEeDAGTLEAL----E 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1546 DIRERVEslSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQ------VAAEKAI--KQAD 1617
Cdd:pfam01576 545 EGKKRLQ--RELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQkkfdqmLAEEKAIsaRYAE 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1618 EDIQGTQNlltSIESETAA---SEEtLFNASQRISELERN-------VEEL---KRKAAQNSGEaeyIEKVVYTVKQSAE 1684
Cdd:pfam01576 623 ERDRAEAE---AREKETRAlslARA-LEEALEAKEELERTnkqlraeMEDLvssKDDVGKNVHE---LERSKRALEQQVE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1685 DVKKTLDgELDEKYKKVE--------NLIAKKT---------EESADARRKA------EM---LQNEAK--TLLAQANSK 1736
Cdd:pfam01576 696 EMKTQLE-ELEDELQATEdaklrlevNMQALKAqferdlqarDEQGEEKRRQlvkqvrELeaeLEDERKqrAQAVAAKKK 774
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 167614504 1737 LQL-LKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDI 1775
Cdd:pfam01576 775 LELdLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQREL 814
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
820-863 |
1.21e-12 |
|
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: 63.91 E-value: 1.21e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 820 PCECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPS 863
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
4.05e-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: 62.37 E-value: 4.05e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRAC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1132-1171 |
1.02e-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: 61.22 E-value: 1.02e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 167614504 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSG 1171
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
821-864 |
1.39e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 1.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 821 CECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWG--FPSC 864
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-512 |
2.89e-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: 60.06 E-value: 2.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 458 CACNPLGTIPGGnpCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLdgcrPCDC 512
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-455 |
3.68e-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: 59.67 E-value: 3.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 398 CTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDLSSEDPFGC 455
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-508 |
4.63e-11 |
|
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: 59.29 E-value: 4.63e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 167614504 457 SCACNPLGTIPGGnpCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLDGCR 508
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1132-1176 |
5.42e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 5.42e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGV-FPDC 1176
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1131-1180 |
7.93e-11 |
|
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: 58.90 E-value: 7.93e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1131 ACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCH 1180
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1456-1691 |
8.30e-11 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 64.61 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDillktnaTKEKMDKSNEELRNLIKQIRNfLTQDSADLD---------------- 1519
Cdd:smart00283 39 ANADEIAATAQSAAEAAEEGREAVED-------AITAMDQIREVVEEAVSAVEE-LEESSDEIGeivsviddiadqtnll 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 ----SIEA------------VANEVlkmempstpqqlQNLTEdirervESlsqvevilQHSAADIAraEMLLEEAKRASK 1583
Cdd:smart00283 111 alnaAIEAarageagrgfavVADEV------------RKLAE------RS--------AESAKEIE--SLIKEIQEETNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1584 SATDVKVTADMVKEALEEAEKAqvaaekaiKQADEDI-QGTQNLLTSIESETAASEETlfnaSQRISELERNVEELKRKA 1662
Cdd:smart00283 163 AVAAMEESSSEVEEGVELVEET--------GDALEEIvDSVEEIADLVQEIAAATDEQ----AAGSEEVNAAIDEIAQVT 230
|
250 260
....*....|....*....|....*....
gi 167614504 1663 AQNSGEAEYIEKVVYTVKQSAEDVKKTLD 1691
Cdd:smart00283 231 QETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1126 |
1.00e-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: 58.52 E-value: 1.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 1083 PCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPD 1126
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1028-1082 |
2.46e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 2.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQLASGTGCD 1082
Cdd:pfam00053 1 CDCNPHGSLSD-------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
509-548 |
3.34e-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: 56.98 E-value: 3.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 167614504 509 PCDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYY 548
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1129 |
4.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVEC 1129
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1218-1774 |
5.58e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 64.85 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1218 ETVDSVERKVSEIKDILA--QSPAAEPLKNIGNLFEEAekliKDVTEMMAQVE---VKlSDTTSQSNSTAKELDSLQTEA 1292
Cdd:NF041483 768 ELVSAAEQTAQQVRDSVAglQEQAEEEIAGLRSAAEHA----AERTRTEAQEEadrVR-SDAYAERERASEDANRLRREA 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1293 ESLDNTVKELAEqlefiknsdiRGALDSITKYFQMSLEAEE---RVNASTTEPNSTVEQSAlMRDRVEdvmmERESQFKE 1369
Cdd:NF041483 843 QEETEAAKALAE----------RTVSEAIAEAERLRSDASEyaqRVRTEASDTLASAEQDA-ARTRAD----AREDANRI 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1370 KQE--EQA-RLLDELAGKLQSLDLSAAAEMTCGTppgascSETECGGPNCRTDEGERKcggpgcgglvtvahnawqkamd 1446
Cdd:NF041483 908 RSDaaAQAdRLIGEATSEAERLTAEARAEAERLR------DEARAEAERVRADAAAQA---------------------- 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1447 lDQDVLSALAEVEQLSkmvSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLikqirnflTQDSAD--LDSIEAV 1524
Cdd:NF041483 960 -EQLIAEATGEAERLR---AEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE--------AREEADrtLDEARKD 1027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANevlkmempstpqqlqnltediRERVESLSQVEVILQHSAADiarAEMLLEEAK-RASKSATDVKVTAD-MVKEALEEA 1602
Cdd:NF041483 1028 AN---------------------KRRSEAAEQADTLITEAAAE---ADQLTAKAQeEALRTTTEAEAQADtMVGAARKEA 1083
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1603 EKAQVAA--------EKAIKQADEDIQGTQNLLTSIESETaasEEtlfnasQRiSELERNVEELKRKAAqnsgeaeyiek 1674
Cdd:NF041483 1084 ERIVAEAtvegnslvEKARTDADELLVGARRDATAIRERA---EE------LR-DRITGEIEELHERAR----------- 1142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1675 vvytvKQSAEDVKKTldGEldekykKVENLIAKKTEESADARRKAEMLQNEA-----KTLLAQANSKLQLLKDLERKYED 1749
Cdd:NF041483 1143 -----RESAEQMKSA--GE------RCDALVKAAEEQLAEAEAKAKELVSDAnseasKVRIAAVKKAEGLLKEAEQKKAE 1209
|
570 580
....*....|....*....|....*.
gi 167614504 1750 NQRyledKAQEL-ARLEGEVRSLLKD 1774
Cdd:NF041483 1210 LVR----EAEKIkAEAEAEAKRTVEE 1231
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
510-554 |
5.67e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.67e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167614504 510 CDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYYFATLDH 554
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
867-914 |
5.69e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 5.69e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167614504 867 CQCNGHA---DDCDPVTGECLnCQDYTMGHNCERCLAGYYGDPiIGSGDHC 914
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
866-911 |
1.60e-09 |
|
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: 55.05 E-value: 1.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 866 PCQCNGHAD---DCDPVTGECLnCQDYTMGHNCERCLAGYYGDPIIGSG 911
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-501 |
1.61e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 458 CACNPLGTIpgGNPCDSETGHCYCKRLVTGQHCDQCLPEHWGLS 501
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1028-1081 |
2.21e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 2.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQlASGTGC 1081
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1028-1081 |
2.99e-09 |
|
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: 54.28 E-value: 2.99e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQLAS-GTGC 1081
Cdd:cd00055 2 CDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1771 |
9.27e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1459 EQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEElrnlikQIRNFLTQDSA-DLDSIEAVANEVLKM---EMP 1534
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE------KARTVAAEDTAaQLAKAARTAEEVLTKaseDAK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1535 STPQQLQNLTEDIRERVESLSQVeviLQHSAADIA--------------RAEM--LLEEAKRASKSATDVKVtadmvkEA 1598
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADR---LRGEAADQAeqlkgaakddtkeyRAKTveLQEEARRLRGEAEQLRA------EA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1599 LEEAEKAQVAAEK-AIKQADEDIQGTQNLLTSIESE--------TAASEETLFNASQRISELERNVEE-LKR---KAAQN 1665
Cdd:NF041483 457 VAEGERIRGEARReAVQQIEEAARTAEELLTKAKADadelrstaTAESERVRTEAIERATTLRRQAEEtLERtraEAERL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1666 SGEAEyiekvvytvkQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADarrKAEMLQNEAKTLLAQANsklQLLKDLER 1745
Cdd:NF041483 537 RAEAE----------EQAEEVRAAAERAARELREETERAIAARQAEAAE---ELTRLHTEAEERLTAAE---EALADARA 600
|
330 340 350
....*....|....*....|....*....|
gi 167614504 1746 KYEdnqRYLEDKAQELARLEGE----VRSL 1771
Cdd:NF041483 601 EAE---RIRREAAEETERLRTEaaerIRTL 627
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-456 |
2.18e-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: 2.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 397 RCTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDLSSeDPFGCK 456
Cdd:cd00055 1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1252-1772 |
2.60e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1252 EAEKLIKDVTEMMAQVEV---KLSDTtSQSNSTAKELDS--LQTEAESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQ 1326
Cdd:NF041483 30 EREKAVQHAEDLGYQVEVlraKLHEA-RRSLASRPAYDGadIGYQAEQLLRNAQIQADQLRADAERELRDARAQTQRILQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1327 MSLEAEERVNAST-TEPNSTveqsalmRDRVEDVMMER----ES----------QFKEKQEEQA-RLLDE---------L 1381
Cdd:NF041483 109 EHAEHQARLQAELhTEAVQR-------RQQLDQELAERrqtvEShvnenvawaeQLRARTESQArRLLDEsraeaeqalA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1382 AGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDeGERkcggpgcggLVTVAHNAWQKAMD-LDQDVLSALAEVEQ 1460
Cdd:NF041483 182 AARAEAERLAEEARQRLGSEAESARAEAEAILRRARKD-AER---------LLNAASTQAQEATDhAEQLRSSTAAESDQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1461 LSKMVSEAKLRADEAKQSAEDILLKTNATKEKM---------------DKSNEE-LRNLIKQIRNFLTQDSADLDSIEAV 1524
Cdd:NF041483 252 ARRQAAELSRAAEQRMQEAEEALREARAEAEKVvaeakeaaakqlasaESANEQrTRTAKEEIARLVGEATKEAEALKAE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANEVLKMEMPSTPQQLQNLTEDIRerveslsqvEVILQHSAADIARAEMLLEEAkrASKSATDVKVTadmVKEALEEAEK 1604
Cdd:NF041483 332 AEQALADARAEAEKLVAEAAEKAR---------TVAAEDTAAQLAKAARTAEEV--LTKASEDAKAT---TRAAAEEAER 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1605 AQVAAE--------KAIKQADEdIQGTQNLLT------SIESETAASE-----ETLfnASQRISELERNVEELKRKAAQN 1665
Cdd:NF041483 398 IRREAEaeadrlrgEAADQAEQ-LKGAAKDDTkeyrakTVELQEEARRlrgeaEQL--RAEAVAEGERIRGEARREAVQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1666 SGE-AEYIEKVVYTVKQSAEDVKKTLDGElDEKYKK--VENLIA--KKTEESAD-ARRKAEMLQNE----AKTLLAQA-N 1734
Cdd:NF041483 475 IEEaARTAEELLTKAKADADELRSTATAE-SERVRTeaIERATTlrRQAEETLErTRAEAERLRAEaeeqAEEVRAAAeR 553
|
570 580 590
....*....|....*....|....*....|....*...
gi 167614504 1735 SKLQLLKDLERKYEDNQrylEDKAQELARLEGEVRSLL 1772
Cdd:NF041483 554 AARELREETERAIAARQ---AEAAEELTRLHTEAEERL 588
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
510-548 |
1.16e-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: 49.66 E-value: 1.16e-07
10 20 30
....*....|....*....|....*....|....*....
gi 167614504 510 CDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYY 548
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-455 |
2.04e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 2.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 398 CTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDlssEDPFGC 455
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1456-1760 |
3.08e-07 |
|
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: 55.40 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDillktnaTKEkmdksnEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPS 1535
Cdd:NF033838 132 KDTLEPGKKVAEATKKVEEAEKKAKD-------QKE------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 TPQQLQNLTEdIRERVESLSQVEVILQHSAADIARAEmllEEAKR---ASKSATDVKVTADMVKEALEEAEKAQVAAEKA 1612
Cdd:NF033838 199 EPRDEEKIKQ-AKAKVESKKAEATRLEKIKTDREKAE---EEAKRradAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1613 IKQADEDiqgtqnllTSIESETAASEETLFNAS----QRISELERNVEELKRKAAQNSGEaeyiekvvyTVKQSAEDVKK 1688
Cdd:NF033838 275 TPDKKEN--------DAKSSDSSVGEETLPSPSlkpeKKVAEAEKKVEEAKKKAKDQKEE---------DRRNYPTNTYK 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1689 TLD---GELDEKYKKVENLIAKktEESADARRKAEMLQNEAK--TLLAQANSKLQLLKDLERKYEDNQRY--LEDKAQE 1760
Cdd:NF033838 338 TLEleiAESDVKVKEAELELVK--EEAKEPRNEEKIKQAKAKveSKKAEATRLEKIKTDRKKAEEEAKRKaaEEDKVKE 414
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1020 |
3.12e-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: 48.50 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167614504 976 CQCHNNIDTTDPeaCDKETGRCLkCLYHTEGEHCQFCRFGYYGDA 1020
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
975-1026 |
1.10e-06 |
|
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: 46.96 E-value: 1.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167614504 975 PCQCHNNIDTtdPEACDKETGRCLkCLYHTEGEHCQFCRFGYYGDALQ-QDCR 1026
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-973 |
3.32e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 3.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 917 CPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNPSEVGGSC 973
Cdd:pfam00053 1 CDCNPHGSLSDT----C--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
867-906 |
4.52e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 4.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167614504 867 CQCN--GHADD-CDPVTGECLnCQDYTMGHNCERCLAGYYGDP 906
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1688-1779 |
5.10e-06 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 48.68 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1688 KTLDGELDEKYKKVENLIAKKteeSADARRKAEMLQNEAKTLLAQANSKLQllKDLERKYEDNQRYLEDKAQELARLEGE 1767
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKL---EKELQALQEKLQKEAATLSEEERQKKE--RELQKKQQELQRKQQEAQQDLQKRQQE 116
|
90
....*....|..
gi 167614504 1768 vrsLLKDISQKV 1779
Cdd:COG2825 117 ---LLQPILEKI 125
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-387 |
6.69e-06 |
|
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: 44.65 E-value: 6.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 335 CNCNEH---SISCHFDmavylatgnvsGGVCDdCQHNTMGRNCEQCKPFYYQHPER 387
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
335-385 |
8.77e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.27 E-value: 8.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 335 CNCNEHSI---SCHFdmavylatgnvSGGVCDdCQHNTMGRNCEQCKPFYYQHP 385
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
271-323 |
1.28e-05 |
|
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: 43.88 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 271 CFCYGHAS---ECAPVDGfneevegmvhgHCMCRHNTKGLNCELCMDFYHDLPWRP 323
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTG-----------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1693-1780 |
2.51e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 45.65 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1693 ELDEKYKKVENLIAKKteeSADARRKAEMLQNEAKTLLAQANSKLQllKDLERKYEDNQRYLEDKAQELARLEGE----V 1768
Cdd:smart00935 22 QLEKEFKKRQAELEKL---EKELQKLKEKLQKDAATLSEAAREKKE--KELQKKVQEFQRKQQKLQQDLQKRQQEelqkI 96
|
90
....*....|..
gi 167614504 1769 RSLLKDISQKVA 1780
Cdd:smart00935 97 LDKINKAIKEVA 108
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-974 |
3.13e-05 |
|
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: 42.73 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 916 PCPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNPSeVGGSCQ 974
Cdd:cd00055 1 PCDCNGHGSLSGQ----C--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1688-1779 |
1.04e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 44.10 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1688 KTLDGELDEKYKKVENLIAKKTEEsadARRKAEMLQNEAKTLLAQansKLQLLKDLERKYEDNQRYLEDKAQELARLEGE 1767
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE---LQKLYEELQKDGALLEEE---REEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
|
90
....*....|..
gi 167614504 1768 vrsLLKDISQKV 1779
Cdd:pfam03938 92 ---LLQPIQDKI 100
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1474-1634 |
1.20e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 44.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1474 EAKQSAEDILLKTNATKEKM--DKSNEELRNLIK-QIRNFLTQDSADLDSI--EAV-ANEVLKMEMPSTPQQLQNLTEDI 1547
Cdd:cd13769 5 ELIQKAQEAINNLAQQVQKQlgLQNPEEVVNTLKeQSDNFANNLQEVSSSLkeEAKkKQGEVEEAWNEFKTKLSETVPEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1548 RERVESLSQVEVILQHSAADIaraEMLLEEAKrasKSATDVKvtadmvkealEEAEKAQVAAEKAIKQA-DEDIQGTQNL 1626
Cdd:cd13769 85 RKSLPVEEKAQELQAKLQSGL---QTLVTESQ---KLAKAIS----------ENSQKAQEELQKATKQAyDIAVEAAQNL 148
|
....*...
gi 167614504 1627 LTSIESET 1634
Cdd:cd13769 149 QNQLQTAT 156
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1019 |
1.31e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.14 E-value: 1.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 976 CQCHNniDTTDPEACDKETGRCLkCLYHTEGEHCQFCRFGYYGD 1019
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-388 |
1.80e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 335 CNCNE---HSISCHFDmavylatgnvsGGVCDdCQHNTMGRNCEQCKPFYYQHPERD 388
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1684-1778 |
6.96e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1684 EDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEML----QNEAKTL----LAQANSKLQLLKDLERKYEDNQryle 1755
Cdd:PRK07353 38 EDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAViaeaEAEADKLaaeaLAEAQAEAQASKEKARREIEQQ---- 113
|
90 100
....*....|....*....|...
gi 167614504 1756 dKAQELARLEGEVRSLLKDISQK 1778
Cdd:PRK07353 114 -KQAALAQLEQQVDALSRQILEK 135
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-966 |
1.63e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 917 CPCpdgpDSGRQFARSCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNP 966
Cdd:smart00180 1 CDC----DPGGSASGTC--DPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-326 |
1.94e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.72 E-value: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 271 CFCYGHASECAPVDgfneevegMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEG 326
Cdd:pfam00053 1 CDCNPHGSLSDTCD--------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| alph_xenorhab_B |
NF033927 |
alpha-xenorhabdolysin family binary toxin subunit B; |
1498-1732 |
2.76e-03 |
|
alpha-xenorhabdolysin family binary toxin subunit B;
Pssm-ID: 411488 [Multi-domain] Cd Length: 223 Bit Score: 41.08 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1498 EELRNLIKQIRNfltqdsadldSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEE 1577
Cdd:NF033927 7 AALRKSAAKIAN----------KLDDLSQINLREATLDLLAQLQEQIAELEAQIAALESKLNELAEDRKVIIEAIDLIEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1578 AKrasksatdvkvTADMVKEAL---EEAEKAQVA-AEKAI-KQAdedIQGTQNLLTSIE-----SETAASEETLfnaSQR 1647
Cdd:NF033927 77 YN-----------IADLFKDLLptaEEIDSLGLPpPEKDLvKAA---IERLKKLLGKISegltyIDLVEARDKL---RDR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1648 ISELERNVEELKRKAAQNSGEAEYIEKVvytvkQSAEDVKKTLDGEldekYKKVEN----LIAKKTEESADarrkaEMLQ 1723
Cdd:NF033927 140 INALLAESRTLDKDIKALAGKLEELTAI-----AAIDEERATWVAE----ARKVEQawesFLDQLTELTSD-----SANL 205
|
....*....
gi 167614504 1724 NEAKTLLAQ 1732
Cdd:NF033927 206 AQLITQLNG 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
35-269 |
1.35e-110 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 350.73 E-value: 1.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 35 CYPATGDLLIGRaqKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICNSQDPYHetlnpdSHLIENVVTTFAPNRLKiWWQS 114
Cdd:pfam00055 1 CYPAFGNLAFGR--EVSATSTCGLNGPERYCILSGLEGGKKCFICDSRDPHN------SHPPSNLTDSNNGTNET-WWQS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 115 ENGV---ENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKTWGVYRYFAYDCEASFpGISTGPMK--KVDDII 189
Cdd:pfam00055 72 ETGViqyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTF-GRPSGPSRgiKDDEVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 190 CDSRYSDIEPSTEGEVIFRAL--DPAFKIEDpYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIReKYYYAVYDMVV 267
Cdd:pfam00055 151 CTSEYSDISPLTGGEVIFSTLegRPSANIFD-YSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISV 228
|
..
gi 167614504 268 RG 269
Cdd:pfam00055 229 GG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
29-269 |
3.02e-84 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 275.78 E-value: 3.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 29 GCAEGSCYPATGDLLIGRaqKLSVTSTCGLHKPEPYCI-VSHLQEDKKCFICNSQDPYHetlnpdSHLIENVVTTFAPNR 107
Cdd:smart00136 1 AGRPRSCYPPFVNLAFGR--EVTATSTCGEPGPERYCKlVGHTEQGKKCDYCDARNPRR------SHPAENLTDGNNPNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 108 LKiWWQSEN---GVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSsDFGKTWGVYRYFAYDCEASFPGISTGPMKK 184
Cdd:smart00136 73 PT-WWQSEPlsnGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 185 V--DDIICDSRYSDIEPSTEGEVIFRALDPAFKIED-PYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYA 261
Cdd:smart00136 151 GneDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDfDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYA 230
|
....*...
gi 167614504 262 VYDMVVRG 269
Cdd:smart00136 231 ISDIAVGG 238
|
|
| cc_LAMB1_C |
cd22300 |
C-terminal coiled-coil domain found in laminin subunit beta-1 (LAMB1); LAMB1 is also called ... |
1714-1786 |
2.45e-39 |
|
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: 140.69 E-value: 2.45e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1714 DARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTCL 1786
Cdd:cd22300 1 DARKKAEMLQNEAKALLAQANSKLQLLKELEKKYEENQKILEDKAQELVGLEEEVRSLLQEISQKVAVYSTCL 73
|
|
| cc_LAMB_C |
cd22295 |
C-terminal coiled-coil domain found in the laminin subunit beta (LAMB) family; The LAMB family ... |
1716-1785 |
2.29e-25 |
|
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: 100.82 E-value: 2.29e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1716 RRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTC 1785
Cdd:cd22295 1 RDRAEKLKKEAEDLLKKANEKLKRLKDLERKFEANEQAMEEKAAELQELEKRVNELLDYIREKVSAYATC 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1224-1778 |
2.25e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1224 ERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKL--------IKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESL 1295
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkaeeKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1296 DNTVKELAEQLEFIKNSDiRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVmmERESQFKEKQEEQA 1375
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAA-EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1376 RLLDEL----AGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKcggpgcgglvtVAHNAWQKAMDLDQ-D 1450
Cdd:PTZ00121 1405 KKADELkkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK-----------KAEEAKKKAEEAKKaD 1473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAE----VEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAV-- 1524
Cdd:PTZ00121 1474 EAKKKAEeakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkk 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANEVLKMEMPSTPQQLQNLTEDireRVESLSQVEVILQHSAADIARAEMLLEEAKRA----SKSATDVKVTADMVKEALE 1600
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeeAKKAEEAKIKAEELKKAEE 1630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1601 E---AEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETlfnaSQRISELERNVEELKRKAAQNSGEAEYIEKVVY 1677
Cdd:PTZ00121 1631 EkkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1678 TVKQSAEDVKKT--LDGELDEKYKKVENLIAKKTEEsadaRRKAEmlqnEAKTLLAQANSKLQLLKDLERKYEDNQRYLE 1755
Cdd:PTZ00121 1707 LKKKEAEEKKKAeeLKKAEEENKIKAEEAKKEAEED----KKKAE----EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
570 580
....*....|....*....|...
gi 167614504 1756 DKAQELARLEGEVRSLLKDISQK 1778
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| cc_LAMB2_C |
cd22299 |
C-terminal coiled-coil domain found in laminin subunit beta-2 (LAMB2); LAMB2 is also called ... |
1715-1785 |
6.35e-19 |
|
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: 82.49 E-value: 6.35e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1715 ARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTC 1785
Cdd:cd22299 1 AKGKAEQLRDEAKGLLQDAQDKLQRLQDLEVQYEENEKVLEGKARQLDGLEDKMKEILKAINQQIQIYNTC 71
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1189-1727 |
4.62e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.89 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1189 IIAELTNRTHRFLEKAKALKISgvigpYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVE 1268
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEK-----IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1269 VKLSDTTSQSNSTAKELDslqtEAESLDNTVKELAEQLEFIKNSdiRGALDSITKYFQMSLEAEERVNA-STTEPNSTVE 1347
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERlKKRLTGLTPE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1348 qsalmrdRVEDVMMERESQFKEKQEEQARLLDELAG-KLQSLDLSAAAEmtcgtppgascsetecggpncRTDEGERKCg 1426
Cdd:PRK03918 388 -------KLEKELEELEKAKEEIEEEISKITARIGElKKEIKELKKAIE---------------------ELKKAKGKC- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1427 gPGCGGLVTVAH----------------NAWQKAMDLDQDVLSALAEVEQLSKMVSE-AKLR--ADEAKqSAEDILLKTN 1487
Cdd:PRK03918 439 -PVCGRELTEEHrkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESElIKLKelAEQLK-ELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1488 ATK-----EKMDKSNEELRNLIKQIRNFLTqdsaDLDSIEAVANE--VLKMEMPSTPQQLQNLTEDIRER-VESLSQVEV 1559
Cdd:PRK03918 517 LEElekkaEEYEKLKEKLIKLKGEIKSLKK----ELEKLEELKKKlaELEKKLDELEEELAELLKELEELgFESVEELEE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1560 ILQHsaadiaraemlLEEAKRASKSATDVKvtadmvKEaLEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAA--- 1636
Cdd:PRK03918 593 RLKE-----------LEPFYNEYLELKDAE------KE-LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElek 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1637 --SEETLFNASQRISELERnveELKRKAAqnsgEAEYIEKVVYTVKQSAEDVKKTLDgELDEKYKKVEnLIAKKTEESAD 1714
Cdd:PRK03918 655 kySEEEYEELREEYLELSR---ELAGLRA----ELEELEKRREEIKKTLEKLKEELE-EREKAKKELE-KLEKALERVEE 725
|
570
....*....|...
gi 167614504 1715 ARRKAEMLQNEAK 1727
Cdd:PRK03918 726 LREKVKKYKALLK 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1285-1775 |
1.53e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.33 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1285 LDSLQTEAESLDNTVKELAEQLEFIKNSdiRGALDSITKYFQMSLEAEERVNASTTEPNSTVEQSALMRDRVEDVMMERE 1364
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARET--RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1365 SQFKEKQEEQARLLDELAgkLQSLDLSAAAEmtcgtppgascsetecggpncRTDEGERKcggpgcggLVTVAhnawQKA 1444
Cdd:PRK02224 286 ERLEELEEERDDLLAEAG--LDDADAEAVEA---------------------RREELEDR--------DEELR----DRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1445 MDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRnfltqdsadlDSIEAV 1524
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE----------ELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANevlkmeMPSTPQQLQNLTEDIRER----VESLSQVEVILQHSAADIARAEMLLEEAK-----RASKSATDVKVTAD-- 1593
Cdd:PRK02224 401 GD------APVDLGNAEDFLEELREErdelREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEdr 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1594 ----MVKEALEEAEKAQVAAEKAIKQAdEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEA 1669
Cdd:PRK02224 475 erveELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1670 EYIEKVVYTVKQSAEDVK---KTLDGELDEKYKKVENL--IAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDL- 1743
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAReevAELNSKLAELKERIESLerIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKr 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1744 ERKYE---------------DNQR---YLEDKAQELARLEGEVRSLLKDI 1775
Cdd:PRK02224 634 ERKREleaefdearieeareDKERaeeYLEQVEEKLDELREERDDLQAEI 683
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
821-869 |
4.62e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 73.54 E-value: 4.62e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 821 CECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPSCQPCQC 869
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1778 |
2.55e-15 |
|
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: 79.81 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1559 VILQHSAADIARAEMLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAEL----------EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1639 ETLFNASQRISELERNVEELKRK------AAQNSGEAEYIE------------KVVYTVKQSAEDVKKTLDgELDEKYKK 1700
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEElaellrALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAE-ELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1701 VENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1454-1769 |
2.62e-15 |
|
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: 82.04 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1454 ALAEVEQLSKMVSEAKLRADEAKQSAEDiLLKTNATKEKMDKSNEELRN-----LIKQIRNFLTQdsadldsIEAVANEV 1528
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLER-LRREREKAERYQALLKEKREyegyeLLKEKEALERQ-------KEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1529 LKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAADIAR---AEMLLEEAKRASKSAtDVKVTADMVKEALEEAEKA 1605
Cdd:TIGR02169 247 ASLE-----EELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeEEQLRVKEKIGELEA-EIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1606 QVAAEKA----------IKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQnsgEAEYIEKV 1675
Cdd:TIGR02169 321 EERLAKLeaeidkllaeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---YREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1676 vytvKQSAEDVKKTLDGELDEKYK----------KVENLIAKKTE---ESADARRKAEMLQNEAKTLLAQANSKLQLLKD 1742
Cdd:TIGR02169 398 ----KREINELKRELDRLQEELQRlseeladlnaAIAGIEAKINEleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340
....*....|....*....|....*..
gi 167614504 1743 LERKYEDNQRYLEDKAQELARLEGEVR 1769
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
773-818 |
3.67e-15 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 70.80 E-value: 3.67e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGC 818
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1229-1771 |
8.62e-15 |
|
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: 80.50 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1229 EIKDILAQSPA-AEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQ-- 1305
Cdd:TIGR02169 428 AIAGIEAKINElEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvr 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1306 ----LEFIKNSDIRGALDSIT---KY---FQMSLE--AEERVNASTTEPNSTVEQ------------------------- 1348
Cdd:TIGR02169 508 ggraVEEVLKASIQGVHGTVAqlgSVgerYATAIEvaAGNRLNNVVVEDDAVAKEaiellkrrkagratflplnkmrder 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1349 ---SALMRDRVEDVMM---ERESQFK-------------EKQEEQARLLDE-----LAGKLqsLDLSAAaeMTCGtppga 1404
Cdd:TIGR02169 588 rdlSILSEDGVIGFAVdlvEFDPKYEpafkyvfgdtlvvEDIEAARRLMGKyrmvtLEGEL--FEKSGA--MTGG----- 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1405 scSETECGGP-NCRTDEGErkcggpgcggLVTVAHnawqKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDIL 1483
Cdd:TIGR02169 659 --SRAPRGGIlFSRSEPAE----------LQRLRE----RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1484 LKTNATKEKMDKSNEELRNLikqirnfltqdSADLDSIEaVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQH 1563
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEEL-----------EEDLSSLE-QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1564 SAADIARAEMLLEEAKRASKSAtdvkvtadmvkeALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESetaaseetlfn 1643
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEA------------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----------- 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1644 asqRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDgELDEKYKKVENliakkteesadARRKAEMLQ 1723
Cdd:TIGR02169 848 ---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD-ELEAQLRELER-----------KIEELEAQI 912
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1724 NEAKTLLAQANSKLQLLKDLERKYEDNQRY----------LEDKAQELARLEGEVRSL 1771
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelsLEDVQAELQRVEEEIRAL 970
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
773-821 |
1.36e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 69.30 E-value: 1.36e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 773 CECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPSGCKPC 821
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1541-1777 |
1.42e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1541 QNLT--EDIRE----RVESLS-QVEVILQH----SAADIARAEMLL-------EEAKRASKSATDVKVTADMVKEALEEA 1602
Cdd:COG1196 186 ENLErlEDILGelerQLEPLErQAEKAERYrelkEELKELEAELLLlklreleAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1603 EKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEyiekvvyTVKQS 1682
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE-------ELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1683 AEDVKKTLDgELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELA 1762
Cdd:COG1196 339 LEELEEELE-EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250
....*....|....*
gi 167614504 1763 RLEGEVRSLLKDISQ 1777
Cdd:COG1196 418 RLEEELEELEEALAE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1489-1777 |
2.47e-14 |
|
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: 78.95 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1489 TKEKMDKsNEELRNLIKqirnflTQDsaDLDSIEAVANEVLKmempstpqQLQNL------TEDIRERVESLSQVEVILq 1562
Cdd:TIGR02168 168 SKYKERR-KETERKLER------TRE--NLDRLEDILNELER--------QLKSLerqaekAERYKELKAELRELELAL- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1563 hSAADIARAEMLLEEakrasksatdvkvtadmVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLF 1642
Cdd:TIGR02168 230 -LVLRLEELREELEE-----------------LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1643 NASQRISELERNVEELKRKAAQnsgeaeyiekvvytvkqsAEDVKKTLDGELDEKYKKVENLIakktEESADARRKAEML 1722
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLAN------------------LERQLEELEAQLEELESKLDELA----EELAELEEKLEEL 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1723 QNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQ 1777
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1220-1779 |
2.53e-14 |
|
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: 78.95 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1220 VDSVERKVSEIKDILAQspAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSdttsQSNSTAKELDSLQTEAESLDNTV 1299
Cdd:TIGR02168 435 LKELQAELEELEEELEE--LQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFSEGV 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1300 KEL-AEQLEFiknSDIRGAL-DSIT---KYfQMSLEA--EERVNASTTEPNSTVEQ--SALMRDRVEDVMM--------- 1361
Cdd:TIGR02168 509 KALlKNQSGL---SGILGVLsELISvdeGY-EAAIEAalGGRLQAVVVENLNAAKKaiAFLKQNELGRVTFlpldsikgt 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1362 ---ERESQFKEKQEEQARLLDEL---AGKLQSL------------DLSAAAEMTCGTPPGAscsetecggpNCRTDEGE- 1422
Cdd:TIGR02168 585 eiqGNDREILKNIEGFLGVAKDLvkfDPKLRKAlsyllggvlvvdDLDNALELAKKLRPGY----------RIVTLDGDl 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1423 -RKCG----GPGCGGLVTVAH-----NAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEK 1492
Cdd:TIGR02168 655 vRPGGvitgGSAKTNSSILERrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1493 MDKSNEELRNLIKQIRNfLTQDSADLDSIEAVANEVLKMEMPSTP-------------QQLQNLTEDIRERVESLSQVEV 1559
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELAeaeaeieeleaqiEQLKEELKALREALDELRAELT 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1560 ILQHSAADIA-RAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIE------- 1631
Cdd:TIGR02168 814 LLNEEAANLReRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEealallr 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1632 SETAASEETLFNASQRISELERNVEELKRKAAQnsgeaeyiekvVYTVKQSAEDVKKTLDGELDEKYK----KVENLIAK 1707
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQ-----------LELRLEGLEVRIDNLQERLSEEYSltleEAEALENK 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1708 KTEESADARRKAEMLQNEAK-----TLLAqanskLQLLKDLERKYEDNQRYLEDKAQELARLEG-------EVRSLLKDI 1775
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKelgpvNLAA-----IEEYEELKERYDFLTAQKEDLTEAKETLEEaieeidrEARERFKDT 1037
|
....
gi 167614504 1776 SQKV 1779
Cdd:TIGR02168 1038 FDQV 1041
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
772-819 |
3.11e-14 |
|
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: 68.53 E-value: 3.11e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 772 ACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGF--GPSGCK 819
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpsQGGGCQ 50
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1467-1778 |
7.04e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1467 EAKLRADEAKQSAEDillktnATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEA-VANEVLKMEMPSTPQQLQNlTE 1545
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEArKADELKKAEEKKKADEAKK-AE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1546 DIRERVEslsqveviLQHSAADIARAEMLLEEAKRASKSATDVKvtadmvKEALEEAEKAQVAAEKAIKQADEdiqgtqn 1625
Cdd:PTZ00121 1300 EKKKADE--------AKKKAEEAKKADEAKKKAEEAKKKADAAK------KKAEEAKKAAEAAKAEAEAAADE------- 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1626 lltsieseTAASEETLFNASQRISELERNVEELKRKAAQNSgEAEYIEKVVYTVKQSAEDVKKTLDG--ELDEKYKKVEN 1703
Cdd:PTZ00121 1359 --------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAkkKADEAKKKAEE 1429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1704 LiaKKTEES---ADARRKAEmlqnEAKTLLAQANSKLQLLKDLE--RKYEDNQRYLED--KAQELARLEGEVRSLLKDIS 1776
Cdd:PTZ00121 1430 K--KKADEAkkkAEEAKKAD----EAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEakKADEAKKKAEEAKKKADEAK 1503
|
..
gi 167614504 1777 QK 1778
Cdd:PTZ00121 1504 KA 1505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1449-1780 |
8.73e-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: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1449 QDVLSALAE-VEQLSKMVSEAK----LRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEA 1523
Cdd:COG1196 192 EDILGELERqLEPLERQAEKAEryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1524 VANEVLKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKrasksatdvkvtadmvkEALEEAE 1603
Cdd:COG1196 272 LRLELEELE-----LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-----------------EELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1604 KAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQnsgeaeyiekvvytvkqsa 1683
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE------------------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1684 edvkktldgELDEKYKKVENLIAKKTEESADARRKAEMLQnEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELAR 1763
Cdd:COG1196 391 ---------ALRAAAELAAQLEELEEAEEALLERLERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
330
....*....|....*..
gi 167614504 1764 LEGEVRSLLKDISQKVA 1780
Cdd:COG1196 461 LLELLAELLEEAALLEA 477
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1217-1783 |
1.03e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1217 RETVDSVERKVSEIKDI-LAQSPAAEPLKNIGNLFEEAEKLIK---DVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEA 1292
Cdd:PRK03918 144 DESREKVVRQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1293 ESLDNTVKELAEQLEFIKNSDIRgaLDSITKyfqmSLEA-EERVNASTTEPNSTVEQSALMRDRVEDV--------MMER 1363
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKE--LESLEG----SKRKlEEKIRELEERIEELKKEIEELEEKVKELkelkekaeEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1364 ESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTcgtppGASCSETECGGPNCRTDEGERKcggpgcgglvtvaHNAWQK 1443
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-----ELEEKEERLEELKKKLKELEKR-------------LEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1444 AMDLDQDVLSALAEVEQLSKMvseaklRADEAKQSAEDILLKTNATKEKMDksnEELRNLIKQIRNfLTQDSADL-DSIE 1522
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKR------LTGLTPEKLEKELEELEKAKEEIE---EEISKITARIGE-LKKEIKELkKAIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1523 AvanevLKMEMPSTPQQLQNLTEDirERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDV----------KVTA 1592
Cdd:PRK03918 430 E-----LKKAKGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkkeseliklKELA 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1593 DMVKEALEEAEKaqVAAEKaIKQADEDIQGTQNLLTSIESETAASEETLfnasQRISELERNVEELKRKaaqnsgeaeyi 1672
Cdd:PRK03918 503 EQLKELEEKLKK--YNLEE-LEKKAEEYEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKK----------- 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1673 ekvvytvkqsaedvKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLaqaNSKlQLLKDLERKYEDNQR 1752
Cdd:PRK03918 565 --------------LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK---DAE-KELEREEKELKKLEE 626
|
570 580 590
....*....|....*....|....*....|.
gi 167614504 1753 YLEDKAQELARLEGEVRSLLKDISQKVAVYS 1783
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1437-1780 |
1.50e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1437 AHNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMD---KSNEELRNlIKQIRNFLTQ 1513
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakKKAEEKKK-ADEAKKKAEE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1514 DSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEViLQHSAADIARAEMLLEEAKRASKsatdvkvtAD 1593
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKK--------AD 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1594 MVKEALEEAEKAQVA---AEKAIKQADEdiqgtqnlLTSIESETAASEETlfnasqRISELERNVEELKRkaAQNSGEAE 1670
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAkkkAEEAKKKADE--------AKKAAEAKKKADEA------KKAEEAKKADEAKK--AEEAKKAD 1537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1671 YIEKVvyTVKQSAEDVKKTLDGELDEKYKKVENliAKKTEESAD-ARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYED 1749
Cdd:PTZ00121 1538 EAKKA--EEKKKADELKKAEELKKAEEKKKAEE--AKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
330 340 350
....*....|....*....|....*....|.
gi 167614504 1750 NQRYLEDKAQELARLEgEVRSLLKDISQKVA 1780
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAE-EEKKKVEQLKKKEA 1643
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1457-1767 |
1.73e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1457 EVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAV--ANEVLKMEMP 1534
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEArkAEDAKKAEAA 1181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1535 STpqqlqnlTEDIReRVESLSQVEVILQHSAADIARAEMLLEEAKRA--SKSATDVKvTADMVKEALEEAEKAQV--AAE 1610
Cdd:PTZ00121 1182 RK-------AEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKAedAKKAEAVK-KAEEAKKDAEEAKKAEEerNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1611 KAIKQADEDIQGTQNLLTSIESETAASEETLFNASQ-------RISELERNVEELKRKaAQNSGEAEYIEKVVYTVKQSA 1683
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkkadeaKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1684 EDVKKTLD--GELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLK---DLERKYEDNQRyledKA 1758
Cdd:PTZ00121 1332 DAAKKKAEeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadEAKKKAEEDKK----KA 1407
|
....*....
gi 167614504 1759 QELARLEGE 1767
Cdd:PTZ00121 1408 DELKKAAAA 1416
|
|
| cc_DmLAMB1-like_C |
cd22302 |
C-terminal coiled-coil domain found in Drosophila melanogaster laminin subunit beta-1 (DmLAMB1) ... |
1716-1785 |
2.01e-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: 66.87 E-value: 2.01e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1716 RRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTC 1785
Cdd:cd22302 1 KERAERLLERASKLANSTSDKLKELQDMEDEFNNNERRLNDLSAEIEELNRRMEGYLEEIERKSEYYRTC 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1187-1775 |
3.21e-13 |
|
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: 75.21 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1187 DVIIAELTNR------THRFLEKAKAlKISGVIGPYRETVDSVERKVSEIKDILAQSpaAEPLKNIGNLFEE--AEK--L 1256
Cdd:pfam01576 186 EAMISDLEERlkkeekGRQELEKAKR-KLEGESTDLQEQIAELQAQIAELRAQLAKK--EEELQAALARLEEetAQKnnA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1257 IKDVTEMMAQVEVKLSDTTSQSNSTAK----------ELDSLQTEAE-SLDNTV--KELAEQLEfIKNSDIRGALDSITK 1323
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAARNKaekqrrdlgeELEALKTELEdTLDTTAaqQELRSKRE-QEVTELKKALEEETR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1324 YFQMSL-EAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEE-----QARLLDE-----LAGKLQSLDlsa 1392
Cdd:pfam01576 342 SHEAQLqEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqQAKQDSEhkrkkLEGQLQELQ--- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1393 aaemtcgtppgASCSETEcggpNCRTDEGERKcgGPGCGGLVTVAHN---AWQKAMDLDQDVLSA---LAEVEQLSKMVS 1466
Cdd:pfam01576 419 -----------ARLSESE----RQRAELAEKL--SKLQSELESVSSLlneAEGKNIKLSKDVSSLesqLQDTQELLQEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1467 EAKLRADEAKQSAEDillKTNATKEKMDKSNEELRNLIKQIRNfLTQDSADLDSieavanevlKME-MPSTPQQLqnltE 1545
Cdd:pfam01576 482 RQKLNLSTRLRQLED---ERNSLQEQLEEEEEAKRNVERQLST-LQAQLSDMKK---------KLEeDAGTLEAL----E 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1546 DIRERVEslSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQ------VAAEKAI--KQAD 1617
Cdd:pfam01576 545 EGKKRLQ--RELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQkkfdqmLAEEKAIsaRYAE 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1618 EDIQGTQNlltSIESETAA---SEEtLFNASQRISELERN-------VEEL---KRKAAQNSGEaeyIEKVVYTVKQSAE 1684
Cdd:pfam01576 623 ERDRAEAE---AREKETRAlslARA-LEEALEAKEELERTnkqlraeMEDLvssKDDVGKNVHE---LERSKRALEQQVE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1685 DVKKTLDgELDEKYKKVE--------NLIAKKT---------EESADARRKA------EM---LQNEAK--TLLAQANSK 1736
Cdd:pfam01576 696 EMKTQLE-ELEDELQATEdaklrlevNMQALKAqferdlqarDEQGEEKRRQlvkqvrELeaeLEDERKqrAQAVAAKKK 774
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 167614504 1737 LQL-LKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDI 1775
Cdd:pfam01576 775 LELdLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQREL 814
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1223-1764 |
5.03e-13 |
|
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: 74.70 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1223 VERKVSEIKDILAQSPAAEplKNIGNLFEEAEKLIKdvtemmAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKEL 1302
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLE--GSSDRILELDQELRK------AERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1303 AEQLEFI-KNSDIRGALDSITK---------YFQMSLEAEERVNASTTEPNSTVEQSAL---------MRDRVEDVMMER 1363
Cdd:TIGR00606 521 DQEMEQLnHHTTTRTQMEMLTKdkmdkdeqiRKIKSRHSDELTSLLGYFPNKKQLEDWLhskskeinqTRDRLAKLNKEL 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1364 ES--QFKEKQEEQARLLDElagklQSLDLSAAAEMTCGtppgasCSETECGGPNCRTD-EGERKCGGPGCGG------LV 1434
Cdd:TIGR00606 601 ASleQNKNHINNELESKEE-----QLSSYEDKLFDVCG------SQDEESDLERLKEEiEKSSKQRAMLAGAtavysqFI 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1435 TVAHNAWQKAMDLDQDVLSALAEVEQLSKMVsEAKLRADEAKQSAEDILLKtnatkeKMDKSNEELRNLIKQIRNfltqd 1514
Cdd:TIGR00606 670 TQLTDENQSCCPVCQRVFQTEAELQEFISDL-QSKLRLAPDKLKSTESELK------KKEKRRDEMLGLAPGRQS----- 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1515 saDLDSIEAvanevlkmEMPSTPQQLQNLTEDIrerveslsqvevilQHSAADIARAEMLLE----EAKRASKSATDVKV 1590
Cdd:TIGR00606 738 --IIDLKEK--------EIPELRNKLQKVNRDI--------------QRLKNDIEEQETLLGtimpEEESAKVCLTDVTI 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1591 TaDMVKEALEEAEK--AQVAAE-------KAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRK 1661
Cdd:TIGR00606 794 M-ERFQMELKDVERkiAQQAAKlqgsdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1662 -------AAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGEL-DEKYKK-----VENLIAKKTEESADARRKAEMLQNEAKt 1728
Cdd:TIGR00606 873 klqigtnLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEkdqqeKEELISSKETSNKKAQDKVNDIKEKVK- 951
|
570 580 590
....*....|....*....|....*....|....*..
gi 167614504 1729 llaqanSKLQLLKDLERKYEDN-QRYLEDKAQELARL 1764
Cdd:TIGR00606 952 ------NIHGYMKDIENKIQDGkDDYLKQKETELNTV 982
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
820-863 |
1.21e-12 |
|
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: 63.91 E-value: 1.21e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 820 PCECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWGFPS 863
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1084-1132 |
4.05e-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: 62.37 E-value: 4.05e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRAC 1132
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| cc_LAMB4_C |
cd22301 |
C-terminal coiled-coil domain found in laminin subunit beta-4 (LAMB4); LAMB4, also called ... |
1718-1785 |
4.28e-12 |
|
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: 63.14 E-value: 4.28e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1718 KAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTC 1785
Cdd:cd22301 3 RLKNIKKEAENLAKEIEDKMKRIEDLEKRIQDLNKRKEDKANQLARLEKQVISLRKEIVERVEGYSTC 70
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1202-1682 |
5.64e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1202 EKAKALKISGVIGP-YRETVDSVERKVSEIKDILAQ-SPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVE--VKLSDTTSQ 1277
Cdd:COG4717 54 EADELFKPQGRKPElNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1278 SNSTAKELDSLQTEAESLDNTVKELAEQLEfiknsDIRGALDSITKYFQmSLEAEERVNASTTEpnSTVEQSALMRDRVE 1357
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEE-----ELEELEAELAELQE-ELEELLEQLSLATE--EELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1358 DVMMERESQFKEKQEEQARL---LDELAGKLQSLDLSAAAEMTCGTPPGAScsetecggpncrtdegeRKCGGPGCGGLV 1434
Cdd:COG4717 206 QRLAELEEELEEAQEELEELeeeLEQLENELEAAALEERLKEARLLLLIAA-----------------ALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1435 TVAHNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKlrADEAKQSAEDILLKTNATKEKMDK-------SNEELRNLIKQI 1507
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE--AEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1508 RNFLTQDSADLDSIEAVANEVLKMEMpstpQQLQNLT-----EDIRERVESLSQVEVILQhsaaDIARAEMLLEEAKRAS 1582
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEI----AALLAEAgvedeEELRAALEQAEEYQELKE----ELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1583 KSATDvKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLtsiesETAASEETLFNASQRISELERNVEELKRKA 1662
Cdd:COG4717 419 EELLE-ALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQELEELKAELRELAEEW 492
|
490 500
....*....|....*....|
gi 167614504 1663 AQNSGEAEYIEKVVYTVKQS 1682
Cdd:COG4717 493 AALKLALELLEEAREEYREE 512
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1247-1769 |
7.33e-12 |
|
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: 70.97 E-value: 7.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1247 GNLFEEAEKL-----IKDVTE-MMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEfiknsDIRGALDS 1320
Cdd:pfam01576 166 SNLAEEEEKAkslskLKNKHEaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA-----ELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1321 ITKYFQMSL-EAEERVNASTTEPNSTVEQSALMRDRVEDvmMERESQFKEKQEEQARLLDE----LAGKLQ-SLDLSAAA 1394
Cdd:pfam01576 241 KEEELQAALaRLEEETAQKNNALKKIRELEAQISELQED--LESERAARNKAEKQRRDLGEeleaLKTELEdTLDTTAAQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1395 -EMTcgtppgaSCSETECGGPNcRTDEGERKcggpgcgglvtvAHNAwqKAMDLDQDVLSALAEV-EQLSKmvseaklrA 1472
Cdd:pfam01576 319 qELR-------SKREQEVTELK-KALEEETR------------SHEA--QLQEMRQKHTQALEELtEQLEQ--------A 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1473 DEAKQSAEDillktnaTKEKMDKSNEELrnlikqirnfltqdSADLDSIEAVANEV----LKMEmpstpQQLQNL----T 1544
Cdd:pfam01576 369 KRNKANLEK-------AKQALESENAEL--------------QAELRTLQQAKQDSehkrKKLE-----GQLQELqarlS 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1545 EDIRERVESLSQVeVILQhsaADIARAEMLLEEA-KRASKSATDV-KVTADM--VKEALEEAEKAQVAAEKAIKQADEDI 1620
Cdd:pfam01576 423 ESERQRAELAEKL-SKLQ---SELESVSSLLNEAeGKNIKLSKDVsSLESQLqdTQELLQEETRQKLNLSTRLRQLEDER 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1621 QGTQNLLTSIESETAASEETLFNASQRISELERNVEElkrkaaqnsgEAEYIEkvvytvkqSAEDVKKTLDGELDEKYKK 1700
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE----------DAGTLE--------ALEEGKKRLQRELEALTQQ 560
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 1701 VEnliaKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYED-NQRYLEDK------AQELARLEGEVR 1769
Cdd:pfam01576 561 LE----EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfDQMLAEEKaisaryAEERDRAEAEAR 632
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1539-1782 |
8.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1539 QLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATdvkvtadmvkEALEEAEKAQVAAEKAIKQADE 1618
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----------LELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLD---GELD 1695
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAeaeEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1696 EKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQL---LKDLERKYEDNQRYLEDKAQELARLEGEVRSLL 1772
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELeeaLAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250
....*....|
gi 167614504 1773 KDISQKVAVY 1782
Cdd:COG1196 463 ELLAELLEEA 472
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1199-1774 |
8.73e-12 |
|
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: 70.38 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1199 RFLEKAKAL-----KISGVIGPYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTE----MMAQVEV 1269
Cdd:TIGR00618 294 PLAAHIKAVtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvatsIREISCQ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1270 KLSDT-------------TSQSNSTAKELDSLQTEAEsldntvKELAEQLEFiknSDIRGALDSITKYFQMSLEAEERVN 1336
Cdd:TIGR00618 374 QHTLTqhihtlqqqkttlTQKLQSLCKELDILQREQA------TIDTRTSAF---RDLQGQLAHAKKQQELQQRYAELCA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1337 ASTTEpnstVEQSALMRDRVEDVMME--RESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTCgtPPGASCSETECG-- 1412
Cdd:TIGR00618 445 AAITC----TAQCEKLEKIHLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC--PLCGSCIHPNPArq 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1413 -----GPNCRtdegerkcggPGCGGLVTVAHnawqkamdLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTN 1487
Cdd:TIGR00618 519 didnpGPLTR----------RMQRGEQTYAQ--------LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1488 ATKEKMDKsneeLRNLIKQIRNfLTQDSADLDSIEAVANEVLKMEMpSTPQQLQNLTEDIRERVESLSQVEVILQHSAAD 1567
Cdd:TIGR00618 581 RSKEDIPN----LQNITVRLQD-LTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1568 IARAEMllEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKaikqadEDIQGTQNLLTSIEsetaaseetlfnasQR 1647
Cdd:TIGR00618 655 LTQERV--REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK------EMLAQCQTLLRELE--------------TH 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1648 ISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTldgeldekykkvenliAKKTEESADARRkaemlqNEAK 1727
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART----------------VLKARTEAHFNN------NEEV 770
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 167614504 1728 TLLAQANSKLQllkDLERKYEDNQRYLEDKAQELARLEGEVRSLLKD 1774
Cdd:TIGR00618 771 TAALQTGAELS---HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS 814
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1132-1171 |
1.02e-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: 61.22 E-value: 1.02e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 167614504 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSG 1171
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYG 40
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1445-1781 |
1.35e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 68.39 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1445 MDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAV 1524
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANEVLKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDvKVTADMVKEALEEAEK 1604
Cdd:COG4372 107 QEEAEELQ-----EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE-ELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1605 AQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRI--SELERNVEELKRKAAQNSGEAEYIEKVVYTVKQS 1682
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKdsLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1683 AEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELA 1762
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|....*....
gi 167614504 1763 RLEGEVRSLLKDISQKVAV 1781
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELL 359
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
821-864 |
1.39e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 1.39e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 821 CECHLQGSVNAFCNPVTGQCHCFQGVYARQCDRCLPGHWG--FPSC 864
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1459-1768 |
1.63e-11 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 68.00 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1459 EQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAvanevlkmEMPSTPQ 1538
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE--------ELEQARS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1539 QLQNLTEDIRERVESLSQVEVILQHSAADIARAEmllEEAKRAsksatdvkvtadmvKEALEEAEKAQVAAEKAIKQADE 1618
Cdd:COG4372 74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQ---EEAEEL--------------QEELEELQKERQDLEQQRKQLEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKrkaaqnsgEAEYIEKVVYTVKQSAEDVKKTLDGELDEKY 1698
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS--------EAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1699 KKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEV 1768
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1455-1780 |
1.71e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1455 LAEVEQLSKMVSEAKLRADEAKQsAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLtQDSADLDSIEAvanevLKMEMP 1534
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEA-----LEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1535 STPQQLQNLtediRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSAT-----DVKVTADMVKEALEEAEKAQVAA 1609
Cdd:COG4717 143 ELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeelqDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1610 EKAIKQADEDIQGTQNLLTSIESETAASEE-----------TLFNASQRISELERNVEE---------------LKRKAA 1663
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIAGvlflvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1664 QNSGEAEYIEKVVYTVKQSAEDVKKTLD----------GELDEKYKKVENLIAKKTE-ESADARRKAEMLQNEAKTLLAQ 1732
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAalglppdlspEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 167614504 1733 ANSKlqLLKDLERKYEDNQRYLEDKaQELARLEGEVRSLLKDISQKVA 1780
Cdd:COG4717 379 AGVE--DEEELRAALEQAEEYQELK-EELEELEEQLEELLGELEELLE 423
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1192-1773 |
2.06e-11 |
|
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: 69.38 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1192 ELTNRTHRfLEKAKALK------ISGVIGPYRETVDSVERKVSEIKDILAQspaaeplknignlFEEAEKliKDVTEMMA 1265
Cdd:pfam15921 146 QLQNTVHE-LEAAKCLKedmledSNTQIEQLRKMMLSHEGVLQEIRSILVD-------------FEEASG--KKIYEHDS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1266 QVEVKLSDTTSQSNSTAKELDslqTEAESLDNTVKELAEQLEFIKnSDIRGALDSITKYFQMSLEA------------EE 1333
Cdd:pfam15921 210 MSTMHFRSLGSAISKILRELD---TEISYLKGRIFPVEDQLEALK-SESQNKIELLLQQHQDRIEQliseheveitglTE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1334 RVNASTTEPNSTVEQSALMRD--RVEDVMMERE--------SQFKEKQEEQARLLDELAGKLQSLDLSAAAEMTcgtppg 1403
Cdd:pfam15921 286 KASSARSQANSIQSQLEIIQEqaRNQNSMYMRQlsdlestvSQLRSELREAKRMYEDKIEELEKQLVLANSELT------ 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1404 ascsetecggpNCRTDEGERKcggpgcgglvtvahnawQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDIL 1483
Cdd:pfam15921 360 -----------EARTERDQFS-----------------QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNS 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1484 LKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAV---ANEVLKmEMPSTPQQLQNLTEDIRERVESLSQVEVI 1560
Cdd:pfam15921 412 ITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiqgKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMT 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1561 LQHSAADIARAEMLLEEAKRASKsATDVKVTA--DMVKEALEEAEKaqvaaekaIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIE-ATNAEITKlrSRVDLKLQELQH--------LKNEGDHLRNVQTECEALKLQMAEKD 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1639 ETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVV---------YTVKQSAEDVK------KTLDGELdEKYKKVeN 1703
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndrrlelqeFKILKDKKDAKireleaRVSDLEL-EKVKLV-N 639
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1704 LIAKKTEESADARRKAEMLQNEAKTLLAQANSklqllkdLERKYEDNQRYLEDKAQELARLEGEVRSLLK 1773
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTSRNELNS-------LSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
458-512 |
2.89e-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: 60.06 E-value: 2.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 458 CACNPLGTIPGGnpCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLdgcrPCDC 512
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDP----PQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
398-455 |
3.68e-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: 59.67 E-value: 3.68e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 398 CTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDLSSEDPFGC 455
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPET--------GQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
457-508 |
4.63e-11 |
|
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: 59.29 E-value: 4.63e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 167614504 457 SCACNPLGTIPGGnpCDSETGHCYCKRLVTGQHCDQCLPEHWGLSNDLDGCR 508
Cdd:cd00055 1 PCDCNGHGSLSGQ--CDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1132-1176 |
5.42e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 59.25 E-value: 5.42e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 1132 CDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGV-FPDC 1176
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1131-1180 |
7.93e-11 |
|
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: 58.90 E-value: 7.93e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1131 ACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCH 1180
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
1456-1691 |
8.30e-11 |
|
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.
Pssm-ID: 214599 [Multi-domain] Cd Length: 262 Bit Score: 64.61 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDillktnaTKEKMDKSNEELRNLIKQIRNfLTQDSADLD---------------- 1519
Cdd:smart00283 39 ANADEIAATAQSAAEAAEEGREAVED-------AITAMDQIREVVEEAVSAVEE-LEESSDEIGeivsviddiadqtnll 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 ----SIEA------------VANEVlkmempstpqqlQNLTEdirervESlsqvevilQHSAADIAraEMLLEEAKRASK 1583
Cdd:smart00283 111 alnaAIEAarageagrgfavVADEV------------RKLAE------RS--------AESAKEIE--SLIKEIQEETNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1584 SATDVKVTADMVKEALEEAEKAqvaaekaiKQADEDI-QGTQNLLTSIESETAASEETlfnaSQRISELERNVEELKRKA 1662
Cdd:smart00283 163 AVAAMEESSSEVEEGVELVEET--------GDALEEIvDSVEEIADLVQEIAAATDEQ----AAGSEEVNAAIDEIAQVT 230
|
250 260
....*....|....*....|....*....
gi 167614504 1663 AQNSGEAEYIEKVVYTVKQSAEDVKKTLD 1691
Cdd:smart00283 231 QETAAMSEEISAAAEELSGLAEELDELVE 259
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1083-1126 |
1.00e-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: 58.52 E-value: 1.00e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 1083 PCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPD 1126
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1189-1775 |
2.03e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1189 IIAELTNRTHRfLEK--AKALKisgvigpYRETVDSVERK-----VSEIKDILAQspaaepLKNIGNLFEEAEKLIKDVT 1261
Cdd:COG1196 194 ILGELERQLEP-LERqaEKAER-------YRELKEELKELeaellLLKLRELEAE------LEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1262 EMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNsDIRGALDSITKYFQMSLEAEERVNASTTE 1341
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1342 pnstVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDELAGKLQSLDLSAAAEMtcgtppgASCSETEcggpNCRTDEG 1421
Cdd:COG1196 339 ----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-------EALRAAA----ELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1422 ERKcggpgcgglvtvahNAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELR 1501
Cdd:COG1196 404 ELE--------------EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1502 NLIKQIRNFLTQDSADLDSIEAVANEVLKME-------MPSTPQQLQNLTEDIRERVESLSQVEV-------------IL 1561
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEadyegflEGVKAALLLAGLRGLAGAVAVLIGVEAayeaaleaalaaaLQ 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1562 QHSAADIARAEMLLEEAKRASKS-ATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQ--GTQNLLTSIESETAASE 1638
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREadARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1639 ETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRK 1718
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 1719 AEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELAR----------LEGEVRSLLKDI 1775
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdleeLERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1450-1742 |
2.06e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1450 DVLSALAEVEQLSKMVSEAKLRADEA-KQSAEDILLKtNATKEKMDKSNEELRNLIKQirnfLTQDSADLDSIEAVANEV 1528
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAeERLAKLEAEI-DKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1529 LkmempstpQQLQNLTEDIRERVESLSQVEV---ILQHSAADIARAE-MLLEEAKRASKSATDVKVTADMVKEALEEAEK 1604
Cdd:TIGR02169 370 R--------AELEEVDKEFAETRDELKDYREkleKLKREINELKRELdRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1605 AQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAE 1684
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1685 DVKKTLD--GELDEKYkkvenliAKKTEESADARRKAEMLQNEaktllAQANSKLQLLKD 1742
Cdd:TIGR02169 522 GVHGTVAqlGSVGERY-------ATAIEVAAGNRLNNVVVEDD-----AVAKEAIELLKR 569
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1028-1082 |
2.46e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 57.36 E-value: 2.46e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQLASGTGCD 1082
Cdd:pfam00053 1 CDCNPHGSLSD-------TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1534-1783 |
2.52e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1534 PSTPQQLQNLTEDIRERVESLSQVEvilqhsaadiARAEMLLEEAKRASKSATDVKvtadmvkEALEEAEKAQVAAEKAI 1613
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQ----------EELEQLREELEQAREELEQLE-------EELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1614 KQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVytvkQSAEDVKKTLDGE 1693
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI----AEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1694 LDEKYKKVENLiakkteESADARRKAEMLQNEAKTLLAQANSKLQLLKDLE--RKYEDNQRYLEDKAQELARLEGEVRSL 1771
Cdd:COG4372 159 LESLQEELAAL------EQELQALSEAEAEQALDELLKEANRNAEKEEELAeaEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250
....*....|..
gi 167614504 1772 LKDISQKVAVYS 1783
Cdd:COG4372 233 LALSALLDALEL 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1466-1778 |
3.25e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.04 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1466 SEAKLRADeakQSAEDILLKTNATkekMDKSNEELRNLIKQIRnfltqdSADLdsIEAVANEV-LKMEMPSTPQQLQNLT 1544
Cdd:COG3206 55 ASATLLVE---PQSSDVLLSGLSS---LSASDSPLETQIEILK------SRPV--LERVVDKLnLDEDPLGEEASREAAI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1545 EDIRER--VESLSQ---VEVILQHS----AADIARA--EMLLEEAKRASKSATdvKVTADMVKEALEEAEKAQVAAEKAI 1613
Cdd:COG3206 121 ERLRKNltVEPVKGsnvIEISYTSPdpelAAAVANAlaEAYLEQNLELRREEA--RKALEFLEEQLPELRKELEEAEAAL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1614 K--QADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEK--VVYTVKQSAEDVKKT 1689
Cdd:COG3206 199 EefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1690 LDgELDEKYK----KVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLE 1765
Cdd:COG3206 279 LA-ELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE 357
|
330
....*....|....*.
gi 167614504 1766 GEV---RSLLKDISQK 1778
Cdd:COG3206 358 REVevaRELYESLLQR 373
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
509-548 |
3.34e-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: 56.98 E-value: 3.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 167614504 509 PCDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYY 548
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1084-1129 |
4.18e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 4.18e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 167614504 1084 CNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVEC 1129
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1218-1774 |
5.58e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 64.85 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1218 ETVDSVERKVSEIKDILA--QSPAAEPLKNIGNLFEEAekliKDVTEMMAQVE---VKlSDTTSQSNSTAKELDSLQTEA 1292
Cdd:NF041483 768 ELVSAAEQTAQQVRDSVAglQEQAEEEIAGLRSAAEHA----AERTRTEAQEEadrVR-SDAYAERERASEDANRLRREA 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1293 ESLDNTVKELAEqlefiknsdiRGALDSITKYFQMSLEAEE---RVNASTTEPNSTVEQSAlMRDRVEdvmmERESQFKE 1369
Cdd:NF041483 843 QEETEAAKALAE----------RTVSEAIAEAERLRSDASEyaqRVRTEASDTLASAEQDA-ARTRAD----AREDANRI 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1370 KQE--EQA-RLLDELAGKLQSLDLSAAAEMTCGTppgascSETECGGPNCRTDEGERKcggpgcgglvtvahnawqkamd 1446
Cdd:NF041483 908 RSDaaAQAdRLIGEATSEAERLTAEARAEAERLR------DEARAEAERVRADAAAQA---------------------- 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1447 lDQDVLSALAEVEQLSkmvSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLikqirnflTQDSAD--LDSIEAV 1524
Cdd:NF041483 960 -EQLIAEATGEAERLR---AEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE--------AREEADrtLDEARKD 1027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANevlkmempstpqqlqnltediRERVESLSQVEVILQHSAADiarAEMLLEEAK-RASKSATDVKVTAD-MVKEALEEA 1602
Cdd:NF041483 1028 AN---------------------KRRSEAAEQADTLITEAAAE---ADQLTAKAQeEALRTTTEAEAQADtMVGAARKEA 1083
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1603 EKAQVAA--------EKAIKQADEDIQGTQNLLTSIESETaasEEtlfnasQRiSELERNVEELKRKAAqnsgeaeyiek 1674
Cdd:NF041483 1084 ERIVAEAtvegnslvEKARTDADELLVGARRDATAIRERA---EE------LR-DRITGEIEELHERAR----------- 1142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1675 vvytvKQSAEDVKKTldGEldekykKVENLIAKKTEESADARRKAEMLQNEA-----KTLLAQANSKLQLLKDLERKYED 1749
Cdd:NF041483 1143 -----RESAEQMKSA--GE------RCDALVKAAEEQLAEAEAKAKELVSDAnseasKVRIAAVKKAEGLLKEAEQKKAE 1209
|
570 580
....*....|....*....|....*.
gi 167614504 1750 NQRyledKAQEL-ARLEGEVRSLLKD 1774
Cdd:NF041483 1210 LVR----EAEKIkAEAEAEAKRTVEE 1231
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
510-554 |
5.67e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.17 E-value: 5.67e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167614504 510 CDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYYFATLDH 554
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
867-914 |
5.69e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 56.21 E-value: 5.69e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 167614504 867 CQCNGHA---DDCDPVTGECLnCQDYTMGHNCERCLAGYYGDPiIGSGDHC 914
Cdd:pfam00053 1 CDCNPHGslsDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1456-1674 |
6.94e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIrNFLTQDSADLDSIEAVANEVLKmemps 1535
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAELEKEIAELRAELE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 tpQQLQNLTEDIRE--RVESLSQVEVIL-QHSAADIARAEMLLEEAKRASKS-ATDVKVTADMVKEALEEAEKAQVAAEK 1611
Cdd:COG4942 101 --AQKEELAELLRAlyRLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1612 AIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEK 1674
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1355-1771 |
8.64e-10 |
|
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: 64.04 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1355 RVEDVMMERESQF---KEKQEEQARLLDELAGKLQSL---------DLSAAAEMtcgtppgasCSETE------------ 1410
Cdd:pfam01576 2 RQEEEMQAKEEELqkvKERQQKAESELKELEKKHQQLceeknalqeQLQAETEL---------CAEAEemrarlaarkqe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1411 ----CGGPNCRTDEGERKCGGpgcgglvtvAHNAWQKAMDLDQDVLSALAEVE------QLSKMVSEAKLradeaKQSAE 1480
Cdd:pfam01576 73 leeiLHELESRLEEEEERSQQ---------LQNEKKKMQQHIQDLEEQLDEEEaarqklQLEKVTTEAKI-----KKLEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1481 DILLKTNAtKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVAN-----------------------EVLKMEMPSTP 1537
Cdd:pfam01576 139 DILLLEDQ-NSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNkheamisdleerlkkeekgrqelEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQLQNLTEDIRERVE----SLSQVEVILQhsaADIARAEmllEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAI 1613
Cdd:pfam01576 218 TDLQEQIAELQAQIAelraQLAKKEEELQ---AALARLE---EETAQKNNALKKIRELEAQISELQEDLESERAARNKAE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1614 KQADEDIQGTQNLLTSIES---ETAASEETLFNASQRISELERNVEE-----------LKRKAAQNSGE-AEYIEkVVYT 1678
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDtldTTAAQQELRSKREQEVTELKKALEEetrsheaqlqeMRQKHTQALEElTEQLE-QAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1679 VKQSAEDVKKTLDGELDEKYKKVENLIAKKTeESADARRKAEmlqneaktllAQansklqlLKDLERKYEDNQRYLEDKA 1758
Cdd:pfam01576 371 NKANLEKAKQALESENAELQAELRTLQQAKQ-DSEHKRKKLE----------GQ-------LQELQARLSESERQRAELA 432
|
490
....*....|...
gi 167614504 1759 QELARLEGEVRSL 1771
Cdd:pfam01576 433 EKLSKLQSELESV 445
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1244-1773 |
9.48e-10 |
|
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: 63.50 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1244 KNIGNLFEE---AEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKN--SDIRGA- 1317
Cdd:TIGR04523 117 EQKNKLEVElnkLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKniDKIKNKl 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1318 ------LDSITKYFQM--SLEAE-------------------ERVNASTTEPNSTVEQSALMRDRVEDVmmerESQFKEK 1370
Cdd:TIGR04523 197 lklellLSNLKKKIQKnkSLESQiselkkqnnqlkdniekkqQEINEKTTEISNTQTQLNQLKDEQNKI----KKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1371 Q---EEQARLLDELAGKLQSLdlsaaaemtcgtppgascsETEcggpncrtdegerkcggpgcgglVTVAHNawQKAMDL 1447
Cdd:TIGR04523 273 QkelEQNNKKIKELEKQLNQL-------------------KSE-----------------------ISDLNN--QKEQDW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1448 DQDVLSALA----EVEQLSKMVSEAKLRADEAKQSAEDIllktnaTKEKMDKSNE------ELRNLIKQIRNFLTQDSAD 1517
Cdd:TIGR04523 309 NKELKSELKnqekKLEEIQNQISQNNKIISQLNEQISQL------KKELTNSESEnsekqrELEEKQNEIEKLKKENQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1518 LDSIEAVANEVLKMEmpSTPQQLQNLTEDIRERVESL-SQVEVILQhsaadiaRAEMLLEEAKRASKSATDVKVTaDMVK 1596
Cdd:TIGR04523 383 KQEIKNLESQINDLE--SKIQNQEKLNQQKDEQIKKLqQEKELLEK-------EIERLKETIIKNNSEIKDLTNQ-DSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1597 E-------ALEEAEKAQVAA-EKAIKQADEDIQGTQNLLTSIESE-------TAASEETLFNASQRISELERNVEELKRK 1661
Cdd:TIGR04523 453 EliiknldNTRESLETQLKVlSRSINKIKQNLEQKQKELKSKEKElkklneeKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1662 AAQnsgeaeyIEKVVytvkQSAEDVKKTLDGELD-EKYKKVENLIAKKTEEsadarrkaemLQNEAKTLLAqANSKLQ-L 1739
Cdd:TIGR04523 533 KKE-------KESKI----SDLEDELNKDDFELKkENLEKEIDEKNKEIEE----------LKQTQKSLKK-KQEEKQeL 590
|
570 580 590
....*....|....*....|....*....|....
gi 167614504 1740 LKDLERKYEDNQRYLEDKAQELARLEGEVRSLLK 1773
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1485-1696 |
9.61e-10 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 60.81 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1485 KTNATKEKMDKSNEELRNLIKQIRNfltqdsadldsIEAVANEvLKMEMPSTPQQLQNLTEDIR---ERVESlSQVEVIL 1561
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEE-----------AEKRAEK-AEAEVAALNRRIQLLEEELErteERLAE-ALEKLEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1562 QHSAAD-------------------IARAEMLLEEAKRASKSA----TDVKVTADMVKEALEEAEKAQVAAEKAIKQADE 1618
Cdd:pfam00261 69 AEKAADesergrkvlenralkdeekMEILEAQLKEAKEIAEEAdrkyEEVARKLVVVEGDLERAEERAELAESKIVELEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIE-SETAAS------EETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLD 1691
Cdd:pfam00261 149 ELKVVGNNLKSLEaSEEKASeredkyEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELD 228
|
....*
gi 167614504 1692 GELDE 1696
Cdd:pfam00261 229 QTLAE 233
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1590-1778 |
1.00e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1590 VTAD----MVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRK---- 1661
Cdd:COG3883 12 AFADpqiqAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElger 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1662 --AAQNSGE--------------AEYIEKVVYtVKQSAEDVKKTLDgELDEKYKKVENliakkteesadARRKAEMLQNE 1725
Cdd:COG3883 92 arALYRSGGsvsyldvllgsesfSDFLDRLSA-LSKIADADADLLE-ELKADKAELEA-----------KKAELEAKLAE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1726 AKTLLAQANSKLqllKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:COG3883 159 LEALKAELEAAK---AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1545-1776 |
1.17e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1545 EDIRERVESL--------------SQVEVILQ--HSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVA 1608
Cdd:PRK03918 111 SSVREWVERLipyhvflnaiyirqGEIDAILEsdESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1609 AEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELER---NVEELKRKAAQNSGEAEYIEKVVYTVKQSAED 1685
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1686 VKKTLDgELDEKYKKVENLiakktEESADARRKAEMLQNEAKTLLAQANSKL----QLLKDLERKYEDnqryLEDKAQEL 1761
Cdd:PRK03918 271 LKKEIE-ELEEKVKELKEL-----KEKAEEYIKLSEFYEEYLDELREIEKRLsrleEEINGIEERIKE----LEEKEERL 340
|
250
....*....|....*
gi 167614504 1762 ARLEGEVRSLLKDIS 1776
Cdd:PRK03918 341 EELKKKLKELEKRLE 355
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
866-911 |
1.60e-09 |
|
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: 55.05 E-value: 1.60e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 167614504 866 PCQCNGHAD---DCDPVTGECLnCQDYTMGHNCERCLAGYYGDPIIGSG 911
Cdd:cd00055 1 PCDCNGHGSlsgQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
458-501 |
1.61e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.01 E-value: 1.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 458 CACNPLGTIpgGNPCDSETGHCYCKRLVTGQHCDQCLPEHWGLS 501
Cdd:smart00180 1 CDCDPGGSA--SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1451-1674 |
1.82e-09 |
|
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: 61.70 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAEVEQLSKMVSEAKLraDEAKQSAEDILLKTNATKEKMDKSNEELRNL---IKQIRNFLTQDSADLDSIEAVANE 1527
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL--EQLQQEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1528 vLKMEMPSTPQQLQNLTEDIRERVESL------SQVEVIL-QHSAADIARAEMLLEEAKRASKSAtdvkvtADMVKEALE 1600
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALyrlgrqPPLALLLsPEDFLDAVRRLQYLKYLAPARREQ------AEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1601 EAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEK 1674
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1483-1780 |
1.82e-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: 62.73 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1483 LLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEV--LKMEMPSTPQQLQNLTEDIRERVESLSQVEVI 1560
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1561 LQHSAADIARAEMLLEEAKRASKSATDVKV--TADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASE 1638
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1639 ETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKtLDGELDEKYKKVENLIAKKTEESADARRK 1718
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-LNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1719 AEMLQNEAKTLLAQANSK--------------LQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSL---LKDISQKVA 1780
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKeliiknldntreslETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVK 513
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1028-1081 |
2.21e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 54.62 E-value: 2.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQlASGTGC 1081
Cdd:smart00180 1 CDCDPGGSASG-------TCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1028-1081 |
2.99e-09 |
|
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: 54.28 E-value: 2.99e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1028 CVCNYLGTVQEhcngsdcQCDKATGQCLCLPNVIGQNCDRCAPNTWQLAS-GTGC 1081
Cdd:cd00055 2 CDCNGHGSLSG-------QCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1431-1683 |
4.57e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1431 GGLVTVAHnAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELrnlikqirnf 1510
Cdd:COG3883 6 LAAPTPAF-ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1511 ltqdsadldsieAVANEvlkmempstpqQLQNLTEDIRERVESL-------SQVEVILQ-HSAAD-IARAEML------- 1574
Cdd:COG3883 75 ------------AEAEA-----------EIEERREELGERARALyrsggsvSYLDVLLGsESFSDfLDRLSALskiadad 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1575 ---LEEAKRASKSATDVKvtaDMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISEL 1651
Cdd:COG3883 132 adlLEELKADKAELEAKK---AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260 270
....*....|....*....|....*....|..
gi 167614504 1652 ERNVEELKRKAAQNSGEAEYIEKVVYTVKQSA 1683
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1471-1772 |
5.46e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.34 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1471 RADEAKQSAEDILLKTnatKEKMDKSNEELRNLikqirnflTQDSADLDSIEAVANEVLKMEmpstpQQLQNLTEDIRER 1550
Cdd:pfam01576 2 RQEEEMQAKEEELQKV---KERQQKAESELKEL--------EKKHQQLCEEKNALQEQLQAE-----TELCAEAEEMRAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1551 VESLSQ-VEVILQHSAADIA----RAEMLLEEAKRASKSATDVKvtadmvkEALEEAEKA-------QVAAEKAIKQADE 1618
Cdd:pfam01576 66 LAARKQeLEEILHELESRLEeeeeRSQQLQNEKKKMQQHIQDLE-------EQLDEEEAArqklqleKVTTEAKIKKLEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIESETAASEETLFNASQRISELE---RNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELD 1695
Cdd:pfam01576 139 DILLLEDQNSKLSKERKLLEERISEFTSNLAEEEekaKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1696 EKYKKVENL----------IAKKTEE--SADARRKAEMLQneaKTLLAQANSKLQ-----LLKDLER------KYEDNQR 1752
Cdd:pfam01576 219 DLQEQIAELqaqiaelraqLAKKEEElqAALARLEEETAQ---KNNALKKIRELEaqiseLQEDLESeraarnKAEKQRR 295
|
330 340
....*....|....*....|
gi 167614504 1753 yleDKAQELARLEGEVRSLL 1772
Cdd:pfam01576 296 ---DLGEELEALKTELEDTL 312
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1443-1751 |
5.54e-09 |
|
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: 61.13 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1443 KAMDLDQD-VLSALAEVEQLSKMVSEAKlradeakqsaEDILLKTNATKEKMDKSNEE--LRNLIKQIRNfLTQDSADLD 1519
Cdd:COG5185 257 KLVEQNTDlRLEKLGENAESSKRLNENA----------NNLIKQFENTKEKIAEYTKSidIKKATESLEE-QLAAAEAEQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 SIEAVANEVLKMempstpqqLQNLTEDIRERVESLSQVEVILQHSAADIARaemlLEEAKRASKSATDVKVTADMVKEAL 1599
Cdd:COG5185 326 ELEESKRETETG--------IQNLTAEIEQGQESLTENLEAIKEEIENIVG----EVELSKSSEELDSFKDTIESTKESL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 EEA-----EKAQVAA---EKAIKQADEDIQgtqNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEy 1671
Cdd:COG5185 394 DEIpqnqrGYAQEILatlEDTLKAADRQIE---ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1672 iEKVVYTVKQSAEDVKKTL---DGELDEKYKKVENLIAkKTEESADARRKAEMLQNEAKTLLAQANSKLQLLK--DLERK 1746
Cdd:COG5185 470 -DEINRSVRSKKEDLNEELtqiESRVSTLKATLEKLRA-KLERQLEGVRSKLDQVAESLKDFMRARGYAHILAleNLIPA 547
|
....*
gi 167614504 1747 YEDNQ 1751
Cdd:COG5185 548 SELIQ 552
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1615-1780 |
7.29e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 7.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1615 QADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGEL 1694
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1695 DEKYKK------VENLIAkkTEESADARRKAEMLQneakTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEV 1768
Cdd:COG3883 93 RALYRSggsvsyLDVLLG--SESFSDFLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170
....*....|..
gi 167614504 1769 RSLLKDISQKVA 1780
Cdd:COG3883 167 EAAKAELEAQQA 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1449-1774 |
8.52e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1449 QDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDIL-LKTNATKEKMDKSNEELRNLIKQIRNfLTQDSADLDS-IEAVAN 1526
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAE-LEEELEEAQEeLEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1527 EVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKrASKSATDVKVTADMVKEALEEAEKAQ 1606
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF-LVLGLLALLFLLLAREKASLGKEAEE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1607 VAAEKAIKQADEdiQGTQNLLTSIESETAASEETLFNASQRISE---LERNVEELKRKAAQNSGEAEyIEKVVYTVKQSA 1683
Cdd:COG4717 307 LQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEElqeLLREAEELEEELQLEELEQE-IAALLAEAGVED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1684 EDvkktldgELDEKYKKVENLIAKKTE-ESADAR---RKAEMLQNEAKTLLAQANSKLQllkDLERKYEDNQRYLEDKAQ 1759
Cdd:COG4717 384 EE-------ELRAALEQAEEYQELKEElEELEEQleeLLGELEELLEALDEEELEEELE---ELEEELEELEEELEELRE 453
|
330
....*....|....*
gi 167614504 1760 ELARLEGEVRSLLKD 1774
Cdd:COG4717 454 ELAELEAELEQLEED 468
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1459-1771 |
9.27e-09 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 60.61 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1459 EQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEElrnlikQIRNFLTQDSA-DLDSIEAVANEVLKM---EMP 1534
Cdd:NF041483 312 EEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE------KARTVAAEDTAaQLAKAARTAEEVLTKaseDAK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1535 STPQQLQNLTEDIRERVESLSQVeviLQHSAADIA--------------RAEM--LLEEAKRASKSATDVKVtadmvkEA 1598
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADR---LRGEAADQAeqlkgaakddtkeyRAKTveLQEEARRLRGEAEQLRA------EA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1599 LEEAEKAQVAAEK-AIKQADEDIQGTQNLLTSIESE--------TAASEETLFNASQRISELERNVEE-LKR---KAAQN 1665
Cdd:NF041483 457 VAEGERIRGEARReAVQQIEEAARTAEELLTKAKADadelrstaTAESERVRTEAIERATTLRRQAEEtLERtraEAERL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1666 SGEAEyiekvvytvkQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADarrKAEMLQNEAKTLLAQANsklQLLKDLER 1745
Cdd:NF041483 537 RAEAE----------EQAEEVRAAAERAARELREETERAIAARQAEAAE---ELTRLHTEAEERLTAAE---EALADARA 600
|
330 340 350
....*....|....*....|....*....|
gi 167614504 1746 KYEdnqRYLEDKAQELARLEGE----VRSL 1771
Cdd:NF041483 601 EAE---RIRREAAEETERLRTEaaerIRTL 627
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1451-1783 |
1.05e-08 |
|
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: 59.97 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAEVEQLSKMV-SEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQirnfltqdsadLDSIEAVANEvl 1529
Cdd:COG5185 133 LKDELIKVEKLDEIAdIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLL-----------KGISELKKAE-- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1530 kmemPSTPQQLQNLTEDIRERVESLSqvevilqhsaADIARAEMLLEEAKRA----SKSATDVKVTADMVKEALEEAEKa 1605
Cdd:COG5185 200 ----PSGTVNSIKESETGNLGSESTL----------LEKAKEIINIEEALKGfqdpESELEDLAQTSDKLEKLVEQNTD- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1606 qvaaekaIKQadEDIQGTQNLLTSIESETAASEETLFNASQRISELERNV------EELKRKAAQNSGEAEYIEKVVYT- 1678
Cdd:COG5185 265 -------LRL--EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIdikkatESLEEQLAAAEAEQELEESKRETe 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1679 --VKQSAEDVKKTLDGeLDEKYKKVENLIAKKTEESaDARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLED 1756
Cdd:COG5185 336 tgIQNLTAEIEQGQES-LTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLED 413
|
330 340
....*....|....*....|....*..
gi 167614504 1757 KAQELARLEGEVRSLLKDISQKVAVYS 1783
Cdd:COG5185 414 TLKAADRQIEELQRQIEQATSSNEEVS 440
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1442-1778 |
1.07e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1442 QKAMDLDQDVLSALAEV----EQLSKMVSE-AKLRADEAKQSAEDILLKTNATKEK--MDKSNEELRNLIKQIRNFLTqd 1514
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIkndkEQKNKLEVElNKLEKQKKENKKNIDKFLTEIKKKEkeLEKLNNKYNDLKKQKEELEN-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1515 saDLDSIEavaNEVLKMEmpstpqqlQNLTeDIRERveslsqvEVILQHSAADIaraEMLLEEAKRASKSATDVKVTADM 1594
Cdd:TIGR04523 174 --ELNLLE---KEKLNIQ--------KNID-KIKNK-------LLKLELLLSNL---KKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1595 VKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKaaqnsgeaeyIEK 1674
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE----------ISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1675 VvytVKQSAEDVKKTLDGELDEKYKKVENL----------IAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLE 1744
Cdd:TIGR04523 300 L---NNQKEQDWNKELKSELKNQEKKLEEIqnqisqnnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350
....*....|....*....|....*....|....
gi 167614504 1745 RkyeDNQRYLedkaQELARLEGEVRSLLKDISQK 1778
Cdd:TIGR04523 377 K---ENQSYK----QEIKNLESQINDLESKIQNQ 403
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1451-1686 |
1.22e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAEVEQlskmvSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIrnflTQDSADLDSIEAvanEVLK 1530
Cdd:COG3883 9 PTPAFADPQI-----QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKLQA---EIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1531 MEmpstpQQLQNLTEDIRERVESL-------SQVEVILQ-HSAAD-IARAEMLLEEAKRASKSATDVKVTADMVKEALEE 1601
Cdd:COG3883 77 AE-----AEIEERREELGERARALyrsggsvSYLDVLLGsESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1602 AEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQ 1681
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*
gi 167614504 1682 SAEDV 1686
Cdd:COG3883 232 AAAAA 236
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1452-1720 |
1.28e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 58.38 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1452 LSALAE-----VEQLSKMVSEAKlradEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNF------LTQDSADLDS 1520
Cdd:COG1340 38 LKELAEkrdelNAQVKELREEAQ----ELREKRDELNEKVKELKEERDELNEKLNELREELDELrkelaeLNKAGGSIDK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1521 IEAVANEVLKMempstpQQLQNLTEDiRERveslsqvEVILQhsaadIARAEMLLEEAKRASKSATDvkvtadmVKEALE 1600
Cdd:COG1340 114 LRKEIERLEWR------QQTEVLSPE-EEK-------ELVEK-----IKELEKELEKAKKALEKNEK-------LKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1601 EAEKAQVAAEKAIKQADEDIQGTQNLLTSIESetaaseetlfnASQRISELERNVEELKRKAAQNSGEAEYIEKvvyTVK 1680
Cdd:COG1340 168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIE-----------LYKEADELRKEADELHKEIVEAQEKADELHE---EII 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 167614504 1681 QSAEDVKKtLDGELDEKYKKVENliAKKTEESADARRKAE 1720
Cdd:COG1340 234 ELQKELRE-LRKELKKLRKKQRA--LKREKEKEELEEKAE 270
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1558-1768 |
2.07e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 56.37 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1558 EVILQHSaadIARAEMLLEEAKRAS-KSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADED--------IQGTQNLLT 1628
Cdd:COG1842 25 EKMLDQA---IRDMEEDLVEARQALaQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDlarealerKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1629 SIESETAASEETLFNASQRISELERNVEELKRK----AAQnsgeaeyiekvvYTVKQSAEDVKKTLDGEldekykkvenl 1704
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKkdtlKAR------------AKAAKAQEKVNEALSGI----------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1705 iakKTEESADARRKAE--MLQNEAKtllAQANSKLQLLKDLERKYEDnqryLEDKAQ---ELARLEGEV 1768
Cdd:COG1842 159 ---DSDDATSALERMEekIEEMEAR---AEAAAELAAGDSLDDELAE----LEADSEvedELAALKAKM 217
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
397-456 |
2.18e-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: 2.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 397 RCTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDLSSeDPFGCK 456
Cdd:cd00055 1 PCDCNGHGSLS-GQCDPGT--------GQCECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1252-1772 |
2.60e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1252 EAEKLIKDVTEMMAQVEV---KLSDTtSQSNSTAKELDS--LQTEAESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQ 1326
Cdd:NF041483 30 EREKAVQHAEDLGYQVEVlraKLHEA-RRSLASRPAYDGadIGYQAEQLLRNAQIQADQLRADAERELRDARAQTQRILQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1327 MSLEAEERVNAST-TEPNSTveqsalmRDRVEDVMMER----ES----------QFKEKQEEQA-RLLDE---------L 1381
Cdd:NF041483 109 EHAEHQARLQAELhTEAVQR-------RQQLDQELAERrqtvEShvnenvawaeQLRARTESQArRLLDEsraeaeqalA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1382 AGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDeGERkcggpgcggLVTVAHNAWQKAMD-LDQDVLSALAEVEQ 1460
Cdd:NF041483 182 AARAEAERLAEEARQRLGSEAESARAEAEAILRRARKD-AER---------LLNAASTQAQEATDhAEQLRSSTAAESDQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1461 LSKMVSEAKLRADEAKQSAEDILLKTNATKEKM---------------DKSNEE-LRNLIKQIRNFLTQDSADLDSIEAV 1524
Cdd:NF041483 252 ARRQAAELSRAAEQRMQEAEEALREARAEAEKVvaeakeaaakqlasaESANEQrTRTAKEEIARLVGEATKEAEALKAE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 ANEVLKMEMPSTPQQLQNLTEDIRerveslsqvEVILQHSAADIARAEMLLEEAkrASKSATDVKVTadmVKEALEEAEK 1604
Cdd:NF041483 332 AEQALADARAEAEKLVAEAAEKAR---------TVAAEDTAAQLAKAARTAEEV--LTKASEDAKAT---TRAAAEEAER 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1605 AQVAAE--------KAIKQADEdIQGTQNLLT------SIESETAASE-----ETLfnASQRISELERNVEELKRKAAQN 1665
Cdd:NF041483 398 IRREAEaeadrlrgEAADQAEQ-LKGAAKDDTkeyrakTVELQEEARRlrgeaEQL--RAEAVAEGERIRGEARREAVQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1666 SGE-AEYIEKVVYTVKQSAEDVKKTLDGElDEKYKK--VENLIA--KKTEESAD-ARRKAEMLQNE----AKTLLAQA-N 1734
Cdd:NF041483 475 IEEaARTAEELLTKAKADADELRSTATAE-SERVRTeaIERATTlrRQAEETLErTRAEAERLRAEaeeqAEEVRAAAeR 553
|
570 580 590
....*....|....*....|....*....|....*...
gi 167614504 1735 SKLQLLKDLERKYEDNQrylEDKAQELARLEGEVRSLL 1772
Cdd:NF041483 554 AARELREETERAIAARQ---AEAAEELTRLHTEAEERL 588
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1592-1781 |
3.15e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.99 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1592 ADMVK----EALEEAEKAQVAAEKAIKQADEDIQgtqnlltSIESETA---ASEETLfnaSQRISELERNVEELKRKA-- 1662
Cdd:COG1842 7 SDIIRaninALLDKAEDPEKMLDQAIRDMEEDLV-------EARQALAqviANQKRL---ERQLEELEAEAEKWEEKArl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1663 AQNSGE----AEYIEKvvytvKQSAEDVKKTLDGELDEKYKKVENLIAKKTE-ES--ADARRKAEMLQNEAKTllAQANS 1735
Cdd:COG1842 77 ALEKGRedlaREALER-----KAELEAQAEALEAQLAQLEEQVEKLKEALRQlESklEELKAKKDTLKARAKA--AKAQE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1736 KLQ----------LLKDLERkYEDNQRYLEDKAQELARLEGEvRSL---LKDISQKVAV 1781
Cdd:COG1842 150 KVNealsgidsddATSALER-MEEKIEEMEARAEAAAELAAG-DSLddeLAELEADSEV 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1538-1766 |
3.32e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQLQNLTEDIRERV----ESLSQVEVILQHsAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAI 1613
Cdd:COG4913 204 KPIGDLDDFVREYMleepDTFEAADALVEH-FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1614 KQADEDIQGT-QNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEA-EYIEKVVYTVKQSAEDVKKTLD 1691
Cdd:COG4913 283 LWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 1692 gELDEKYKKVEnLIAKKTEES-ADARRKAEMLQNEAKTLLAQANSKLQllkDLERKYEDNQRYLEDKAQELARLEG 1766
Cdd:COG4913 363 -RLEALLAALG-LPLPASAEEfAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLER 433
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1588-1773 |
3.44e-08 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 56.19 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1588 VKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKR--KAAQN 1665
Cdd:pfam00261 6 IKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrKVLEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1666 SgEAEYIEKVVYTVKQSAEdvKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDL-- 1743
Cdd:pfam00261 86 R-ALKDEEKMEILEAQLKE--AKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLea 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 167614504 1744 --------ERKYEDNQRYLEDKAQEL-ARLEGEVRSLLK 1773
Cdd:pfam00261 163 seekaserEDKYEEQIRFLTEKLKEAeTRAEFAERSVQK 201
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1593-1777 |
3.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1593 DMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYI 1672
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1673 EkvVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKtEESADARRKAEMLQNEAKTLLAQ-ANSKLQLLKDLERKYEDNQ 1751
Cdd:COG4717 129 P--LYQELEALEAELAELPERLEELEERLEELRELE-EELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQ 205
|
170 180
....*....|....*....|....*.
gi 167614504 1752 RYLEDKAQELARLEGEVRSLLKDISQ 1777
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQ 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1497-1701 |
6.01e-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: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1497 NEELRNLIK-QirnflTQDSAdLDSIEAVANEVlkmempstPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLL 1575
Cdd:COG1579 3 PEDLRALLDlQ-----ELDSE-LDRLEHRLKEL--------PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1576 EEA----KRASK---SATDVKVTADMVKEaLEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLfnaSQRI 1648
Cdd:COG1579 69 EEVeariKKYEEqlgNVRNNKEYEALQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL---EEKK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1649 SELERNVEELKRKAAQnsgeaeyiekvvytVKQSAEDVKKTLDGELDEKYKKV 1701
Cdd:COG1579 145 AELDEELAELEAELEE--------------LEAEREELAAKIPPELLALYERI 183
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1561-1780 |
7.59e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.97 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1561 LQHSAADIARAEML-LEEAKRASKsatdvkvtADMVKEALEEAEKAQVAAEKAIKQADEdiqgtqnlltsiesetaasee 1639
Cdd:COG3064 5 LEEKAAEAAAQERLeQAEAEKRAA--------AEAEQKAKEEAEEERLAELEAKRQAEE--------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1640 tlfNASQRISELERNVEELKRKAAQNSGEAEyiekvvytvkQSAEDVKKTLDGELDEKYKKVENLIAK-------KTEES 1712
Cdd:COG3064 56 ---EAREAKAEAEQRAAELAAEAAKKLAEAE----------KAAAEAEKKAAAEKAKAAKEAEAAAAAekaaaaaEKEKA 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1713 ADARRKAEM---LQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVA 1780
Cdd:COG3064 123 EEAKRKAEEeakRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAA 193
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1251-1658 |
8.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1251 EEAEKLIKDVTEMMAQVEVKLSDTTSQsnstakeLDSLQTEAESLdNTVKELAEQLEFIKNS----DIRGALDSITKYFQ 1326
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQ-------LKSLERQAEKA-ERYKELKAELRELELAllvlRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1327 MSLEAEERVNASTTEPNSTVEQSALMRDRVEdvmmERESQFKEKQEEqarlLDELAGKLQSLDLSAAaemtcgtppgasc 1406
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVS----ELEEEIEELQKE----LYALANEISRLEQQKQ------------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1407 setecggpncRTDEGERkcggpgcgglvtvahnawqkamDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKT 1486
Cdd:TIGR02168 306 ----------ILRERLA----------------------NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1487 NATKEKMDKSNEELRNLIKQIRNFLTQdsadldsIEAVANEVLKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAA 1566
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLE-----LQIASLNNEIERLEARLERLEDRRERLQQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1567 DIARAEMLLEEAKRAsksatDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAAseetlfnASQ 1646
Cdd:TIGR02168 422 EIEELLKKLEEAELK-----ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-------LQA 489
|
410
....*....|..
gi 167614504 1647 RISELERNVEEL 1658
Cdd:TIGR02168 490 RLDSLERLQENL 501
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1297-1727 |
9.36e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1297 NTVKELAEQLEFIKNSDIRGALDSITKYFQMSLEAEERVNASTTEPNSTV--EQSALMRDRVEDVMMERESQFK------ 1368
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGilKDTELTKLKESAKAKESGLRKGvsleeg 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1369 --EKQEEQARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKCGgpgcgglvtVAHNAWQKAMD 1446
Cdd:pfam02463 658 laEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL---------EAEELLADRVQ 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1447 LDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVAN 1526
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1527 EV-LKMEMPSTPQQLQNLTEDIRERV-ESLSQVEVILQHSA-ADIARAEMLLEEAK----RASKSATDVKVTADMVKEAL 1599
Cdd:pfam02463 809 ELkEEAELLEEEQLLIEQEEKIKEEElEELALELKEEQKLEkLAEEELERLEEEITkeelLQELLLKEEELEEQKLKDEL 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 EEAEKAQVAAEKaikQADEDIQGTQNLLTSIESETAASEETLFNASQRISELER-NVEELKRKAAQNSGEAEYIEKVVYT 1678
Cdd:pfam02463 889 ESKEEKEKEEKK---ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEElLLEEADEKEKEENNKEEEEERNKRL 965
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1679 VKQSAEDVKKTLDG-----ELDEKYKKVENLIAKKTEESADARRKAEMLQNEAK 1727
Cdd:pfam02463 966 LLAKEELGKVNLMAieefeEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
510-548 |
1.16e-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: 49.66 E-value: 1.16e-07
10 20 30
....*....|....*....|....*....|....*....
gi 167614504 510 CDCDLGGALNNSCFAESGQCSCRPHMIGRQCNEVEPGYY 548
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1248-1778 |
1.33e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1248 NLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQT--------EAESlDNTVKELAEQLEFIKNSDirgalD 1319
Cdd:pfam05557 13 QLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKrirllekrEAEA-EEALREQAELNRLKKKYL-----E 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1320 SITKYFQ--MSLEAEervnASTTEPNSTVEQSALMRdRVEDVMMERESQFKEKQEEQARLlDELAGKLQSL-DLSAAAEM 1396
Cdd:pfam05557 87 ALNKKLNekESQLAD----AREVISCLKNELSELRR-QIQRAELELQSTNSELEELQERL-DLLKAKASEAeQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1397 TCgtppgASCSETECggpncRTDEGERKCggpgcgglvtvahnawQKAMDLDQDVLSALAEVEQLSKMVSE-AKLRADEA 1475
Cdd:pfam05557 161 QQ-----SSLAEAEQ-----RIKELEFEI----------------QSQEQDSEIVKNSKSELARIPELEKElERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1476 K--QSAEDILL---KTNATK---EKMDKSNEELRNLikQIRNFLTQdsADLDSIEAVA-NEVLKMEMPstpqqlqnltED 1546
Cdd:pfam05557 215 HlnENIENKLLlkeEVEDLKrklEREEKYREEAATL--ELEKEKLE--QELQSWVKLAqDTGLNLRSP----------ED 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1547 IRERVESLSQVEVIL---------QHSAADIARAEmLLEEAKRASKSATDVK-------------------VTA--DMVK 1596
Cdd:pfam05557 281 LSRRIEQLQQREIVLkeenssltsSARQLEKARRE-LEQELAQYLKKIEDLNkklkrhkalvrrlqrrvllLTKerDGYR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1597 EALEEAEKAQVAAE------KAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNsgEAE 1670
Cdd:pfam05557 360 AILESYDKELTMSNyspqllERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLA--DPS 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1671 YIEKVVYTVKQSAED-------------------VKKTLDGELDEKYKKV----ENLIAKKTEESADarrKAEMLQNEAK 1727
Cdd:pfam05557 438 YSKEEVDSLRRKLETlelerqrlreqknelemelERRCLQGDYDPKKTKVlhlsMNPAAEAYQQRKN---QLEKLQAEIE 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1728 TLLAqansklqLLKDLERKYEDNQRY----LEDKAQELARLEGEVRSL------LKDISQK 1778
Cdd:pfam05557 515 RLKR-------LLKKLEDDLEQVLRLpettSTMNFKEVLDLRKELESAelknqrLKEVFQA 568
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1459-1725 |
1.54e-07 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 55.36 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1459 EQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNL----IKQIRNFLTQDSADLDSIEAVANEVL----- 1529
Cdd:pfam09311 37 DQLEKTMKDKKELEDKMNQLSEETSNQVSTLAKRNQKSETLLDELqqafSQAKRNFQDQLAVLMDSREQVSDELVrlqkd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1530 ------------------KMEMPSTPQQLQNLTEDIRERVESLsqvevilqhsaadiaraemlleeakRASKSATDVKVT 1591
Cdd:pfam09311 117 neslqgkhslhvslqqaeKFDMPDTVQELQELVLKYREELIEV-------------------------RTAADHMEEKLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1592 ADMVkealeeAEKAQVAAEKAIKQADEDiqgtqnlltSIESETAASEETLFNASQRISELERNveelkrKAAQNSGEAEY 1671
Cdd:pfam09311 172 AEIL------FLKEQIQAEQCLKENLEE---------TLQAEIENCKEEIASISSLKVELERI------KAEKEQLENGL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1672 IEKVvytvkQSAEDVkKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNE 1725
Cdd:pfam09311 231 TEKI-----RQLEDL-QTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTE 278
|
|
| cc_LAMB3_C |
cd22303 |
C-terminal coiled-coil domain found in laminin subunit beta-3 (LAMB3); LAMB3 is also called ... |
1722-1785 |
1.60e-07 |
|
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: 50.13 E-value: 1.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1722 LQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQKVAVYSTC 1785
Cdd:cd22303 7 IKKEAESLFKETSDMMKRMKDIETELQEGAQALEGKSARLLGLEEQVEKIRDDINNRVTYYSTC 70
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
398-455 |
2.04e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 2.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 398 CTCDPAGSQNeGICDSYTdfstgliaGQCRCKLNVEGEHCDVCKEGFYDlssEDPFGC 455
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDT--------GQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1440-1670 |
2.11e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1440 AWQKAMDLDQdvLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNfltQDSADLD 1519
Cdd:COG4913 267 ARERLAELEY--LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG---NGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 SIEavanevlkmempstpQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSAtdvkvtADMVKEAL 1599
Cdd:COG4913 342 QLE---------------REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL------LEALEEEL 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1600 EEAEKAQVAAEKAIKQADEDIQGTQNLLTSIEsetaaseetlfnasQRISELERNVEELKRKAAQNSGEAE 1670
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLE--------------RRKSNIPARLLALRDALAEALGLDE 457
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1547-1766 |
2.70e-07 |
|
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: 53.14 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1547 IRERVESLSQVEVILQHSAADiARAEmlLEEAKRASKSA-TDVKVTADMVKEALEEAEKAQVAAEKAIKQADED------ 1619
Cdd:pfam04012 13 IHEGLDKAEDPEKMLEQAIRD-MQSE--LVKARQALAQTiARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEElareal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1620 --IQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKaaqnsgeaeyIEKVVYTVKQ--SAEDVKKTLDGeld 1695
Cdd:pfam04012 90 aeKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----------KNLLKARLKAakAQEAVQTSLGS--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 1696 ekykkvenliaKKTEESADA-----RRKAEMlqnEAktlLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEG 1766
Cdd:pfam04012 157 -----------LSTSSATDSferieEKIEER---EA---RADAAAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1265-1761 |
2.74e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 55.42 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1265 AQVEV---KLSDTTSQSNSTAKELDSLQTEAESLDN---------------------TVKELAeqLEFIKnsdIRGALDS 1320
Cdd:pfam05701 124 AQLEVakaRHAAAVAELKSVKEELESLRKEYASLVSerdiaikraeeavsaskeiekTVEELT--IELIA---TKESLES 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1321 itkyFQMS-LEAEE-RVNAsttepnstveqsALMRDRvEDVMMEREsqFKEKQEEQARLLDEL--AGKLQS--------- 1387
Cdd:pfam05701 199 ----AHAAhLEAEEhRIGA------------ALAREQ-DKLNWEKE--LKQAEEELQRLNQQLlsAKDLKSkletasall 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1388 LDLSA--AAEMTcgtppGASCSETEcggpncrtDEGERKCggpgcgglvtvAHNAWQKAMDldqdvlSALAEVEQLSKMV 1465
Cdd:pfam05701 260 LDLKAelAAYME-----SKLKEEAD--------GEGNEKK-----------TSTSIQAALA------SAKKELEEVKANI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1466 SEAKlraDEAKqsaediLLKTNAT--KEKMDKSNEELRNLikqirnfltQDSADLDSIeAVANevLKMEMPSTPQQL--- 1540
Cdd:pfam05701 310 EKAK---DEVN------CLRVAAAslRSELEKEKAELASL---------RQREGMASI-AVSS--LEAELNRTKSEIalv 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1541 QNLTEDIRERVESLSQvevILQhsaadiaRAEMLLEEAKRASKSATDvkvtadMVKEALEEAEKAQVAAekaikqadedi 1620
Cdd:pfam05701 369 QAKEKEAREKMVELPK---QLQ-------QAAQEAEEAKSLAQAARE------ELRKAKEEAEQAKAAA----------- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1621 qgtqnllTSIESE-TAASEETL-FNASqriselernvEELKRKAAQNSGEAEYIEKvvytvKQSAEDVKK--TLD-GELD 1695
Cdd:pfam05701 422 -------STVESRlEAVLKEIEaAKAS----------EKLALAAIKALQESESSAE-----STNQEDSPRgvTLSlEEYY 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1696 EKYKKvenliAKKTEESADARrkaemlqneaktlLAQANSKLQLLKD-----LERKYEDNqRYLEDKAQEL 1761
Cdd:pfam05701 480 ELSKR-----AHEAEELANKR-------------VAEAVSQIEEAKEselrsLEKLEEVN-REMEERKEAL 531
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1456-1760 |
3.08e-07 |
|
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: 55.40 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDillktnaTKEkmdksnEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPS 1535
Cdd:NF033838 132 KDTLEPGKKVAEATKKVEEAEKKAKD-------QKE------EDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 TPQQLQNLTEdIRERVESLSQVEVILQHSAADIARAEmllEEAKR---ASKSATDVKVTADMVKEALEEAEKAQVAAEKA 1612
Cdd:NF033838 199 EPRDEEKIKQ-AKAKVESKKAEATRLEKIKTDREKAE---EEAKRradAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1613 IKQADEDiqgtqnllTSIESETAASEETLFNAS----QRISELERNVEELKRKAAQNSGEaeyiekvvyTVKQSAEDVKK 1688
Cdd:NF033838 275 TPDKKEN--------DAKSSDSSVGEETLPSPSlkpeKKVAEAEKKVEEAKKKAKDQKEE---------DRRNYPTNTYK 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1689 TLD---GELDEKYKKVENLIAKktEESADARRKAEMLQNEAK--TLLAQANSKLQLLKDLERKYEDNQRY--LEDKAQE 1760
Cdd:NF033838 338 TLEleiAESDVKVKEAELELVK--EEAKEPRNEEKIKQAKAKveSKKAEATRLEKIKTDRKKAEEEAKRKaaEEDKVKE 414
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
976-1020 |
3.12e-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: 48.50 E-value: 3.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 167614504 976 CQCHNNIDTTDPeaCDKETGRCLkCLYHTEGEHCQFCRFGYYGDA 1020
Cdd:pfam00053 1 CDCNPHGSLSDT--CDPETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1452-1752 |
3.16e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1452 LSALAE-VEQLSKMVSEAKLRADE-AKQSAEDIllktnatKEKMDKSnEELRNLIKQIRNFLTQdsadLDSIEAV----- 1524
Cdd:COG3096 866 LDQLKEqLQLLNKLLPQANLLADEtLADRLEEL-------REELDAA-QEAQAFIQQHGKALAQ----LEPLVAVlqsdp 933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1525 -ANEVLKMEMpstpQQLQNLTEDIRERVESLSQVEVILQH-SAADiarAEMLLEEakrasksatdvkvTADMV---KEAL 1599
Cdd:COG3096 934 eQFEQLQADY----LQAKEQQRRLKQQIFALSEVVQRRPHfSYED---AVGLLGE-------------NSDLNeklRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 EEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISEL---------ER---NVEELKRKAAQNSG 1667
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadaeaeERariRRDELHEELSQNRS 1073
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1668 EAEYIEKVVYTVKQSAEDVKKTLdGELDEKY----KKVENliAKKT-----EESADA---RR--KAEMLQNEAKTL---- 1729
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSLQKRL-RKAERDYkqerEQVVQ--AKAGwcavlRLARDNdveRRlhRRELAYLSADELrsms 1150
|
330 340 350
....*....|....*....|....*....|.
gi 167614504 1730 --------LAQANskLQLLKDLERKYEDNQR 1752
Cdd:COG3096 1151 dkalgalrLAVAD--NEHLRDALRLSEDPRR 1179
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1250-1786 |
3.77e-07 |
|
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: 55.44 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1250 FEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNsdirgaLDSITKYFQMSL 1329
Cdd:TIGR00606 205 HQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK------LDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1330 EAEERVNASTTEPNSTVEQSAlmRDRVEDVMMERESQFKEKQEEQARLLDELaGKL-----------------QSLDLSA 1392
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGT--DEQLNDLYHNHQRTVREKERELVDCQREL-EKLnkerrllnqektellveQGRLQLQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1393 AAEMTCGTPpgASCSETECGGPNCRTDEGERkcgGPGCGGLVTVAHNAWQKAMDLDQDVLSAL-AEVEQLSKMVSEA--K 1469
Cdd:TIGR00606 356 ADRHQEHIR--ARDSLIQSLATRLELDGFER---GPFSERQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQadE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1470 LRaDEAKQSAEDILLKtnatKEKMDKSNEELRNLIKQIRNF-------------LTQDSADLDSIEAVAN-EVLKMEMPS 1535
Cdd:TIGR00606 431 IR-DEKKGLGRTIELK----KEILEKKQEELKFVIKELQQLegssdrileldqeLRKAERELSKAEKNSLtETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 tpqqLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKV--TADMVKEALEEAEKAQV-----A 1608
Cdd:TIGR00606 506 ----LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhSDELTSLLGYFPNKKQLedwlhS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1609 AEKAIKQADEDIQGTQ--------------NLLTSIESETAASEETLFNA--SQRI-SELERNVEELKRK-------AAQ 1664
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNkelasleqnknhinNELESKEEQLSSYEDKLFDVcgSQDEeSDLERLKEEIEKSskqramlAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1665 NSGEAEYIEKV-------------VYTVKQSAEDVKKTLDGEL---DEKYKKVENLIAKKTEESADARRKAEMLQNEakt 1728
Cdd:TIGR00606 662 TAVYSQFITQLtdenqsccpvcqrVFQTEAELQEFISDLQSKLrlaPDKLKSTESELKKKEKRRDEMLGLAPGRQSI--- 738
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1729 llaqanskLQLL-KDLERKYEDNQRYLEDKAQELARLEgEVRSLLKDISQKVAVYSTCL 1786
Cdd:TIGR00606 739 --------IDLKeKEIPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCL 788
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1442-1668 |
5.89e-07 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 52.69 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1442 QKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEdillktNATKEKMDKSNEELRNL-IKQIRNFLTQDSADLDS 1520
Cdd:pfam12795 23 QQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELA------ALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1521 IEAVANEV--LKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATdvkvtADMVKEA 1598
Cdd:pfam12795 97 LQNQLAQLnsQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQ-----IDMLEQE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 1599 LE------EAEKAQV-AAEKAIKQADEDIQGTQNLLtsiesetaaseetlfnASQRISELERNVEELKRKAAQNSGE 1668
Cdd:pfam12795 172 LLsnnnrqDLLKARRdLLTLRIQRLEQQLQALQELL----------------NEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1244-1778 |
7.79e-07 |
|
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: 54.28 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1244 KNIGNLFEEAEKLIKDVTEMmaqvEVKLSDTTSQSnstakelDSLQTEAESLDNTVKELAEQLE---FIKNSDIRGALDS 1320
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTEL----LVEQGRLQLQA-------DRHQEHIRARDSLIQSLATRLEldgFERGPFSERQIKN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1321 ITKYFQMSLEAEERV---NASTTEPNSTVEQSALmrDRVEDVM------MERESQFKEKQEEQARL-----------LDE 1380
Cdd:TIGR00606 395 FHTLVIERQEDEAKTaaqLCADLQSKERLKQEQA--DEIRDEKkglgrtIELKKEILEKKQEELKFvikelqqlegsSDR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1381 LAGKLQSLdLSAAAEMtcgtPPGASCSETECGG------PNCRTDEGERKCGGPgcgglvtvahnawQKAMDLDQDVLSa 1454
Cdd:TIGR00606 473 ILELDQEL-RKAEREL----SKAEKNSLTETLKkevkslQNEKADLDRKLRKLD-------------QEMEQLNHHTTT- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1455 LAEVEQLS--KMVSEAKLRADEAKQSAEDI-LLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKm 1531
Cdd:TIGR00606 534 RTQMEMLTkdKMDKDEQIRKIKSRHSDELTsLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN- 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1532 EMPSTPQQLQNLTEDI----------------RERVESLSQVEVILqhsAADIARAEMLLEEAKRASKSATDV------- 1588
Cdd:TIGR00606 613 ELESKEEQLSSYEDKLfdvcgsqdeesdlerlKEEIEKSSKQRAML---AGATAVYSQFITQLTDENQSCCPVcqrvfqt 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1589 -----KVTAD---MVKEALEEAEKAQVAAEKAIKQADEDI---QGTQNLLTSIESETAASEETLFNASQRISELERNVEE 1657
Cdd:TIGR00606 690 eaelqEFISDlqsKLRLAPDKLKSTESELKKKEKRRDEMLglaPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1658 LKRKAAQNSGEAEYIE------KVVYTVKQSAEDVKK-------TLDG-ELDEKYKKVENLIAKKTEESADARRKAEMLQ 1723
Cdd:TIGR00606 770 QETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERkiaqqaaKLQGsDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1724 ---NEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:TIGR00606 850 kliQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
|
| Mt_ATP_synt |
pfam15704 |
Mitochondrial ATP synthase subunit; This plant mitochondrial ATP synthase subunit may the the ... |
1472-1688 |
1.02e-06 |
|
Mitochondrial ATP synthase subunit; This plant mitochondrial ATP synthase subunit may the the equivalent of the mitochondrial ATP synthase d subunit.
Pssm-ID: 406195 [Multi-domain] Cd Length: 188 Bit Score: 50.92 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1472 ADEAKQSAEDILLKtnatkEKMDKSNEELRNLIKQIRNF-LTQDSADLDSIEAVANEVL----KMEMPSTPQQLQNLted 1546
Cdd:pfam15704 4 AAEPKALAGDDVVK-----SVFIEVQKKFRALLGVLRKEkITIDPGDPAAVKAYAAVMKaarkKAGLPSPSQRIKET--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1547 irerveslsqveviLQHSAADIARAEMLLEEAK--RASKSATDVKVTADMVKEALEEAEKaqvAAEKAIKQADEdiQGTQ 1624
Cdd:pfam15704 76 --------------IEGATQEIPDVRTFLEKLGeiRIKRGLEDELGAEALMMEALDKVEK---AIGKPLLRSDK--KGMA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1625 NLltsieseTAASEETLFNASQRISELERNVEELKRKAAQNSgeaeyIEKVVYTVKQSAEDVKK 1688
Cdd:pfam15704 137 LL-------TAEFDKINKKLGIRKEDLPKYEEELELEIAKAE-----LLELKKTALEAMETQKK 188
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
975-1026 |
1.10e-06 |
|
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: 46.96 E-value: 1.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 167614504 975 PCQCHNNIDTtdPEACDKETGRCLkCLYHTEGEHCQFCRFGYYGDALQ-QDCR 1026
Cdd:cd00055 1 PCDCNGHGSL--SGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1484-1738 |
1.26e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 52.51 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1484 LKTNATKEkmDKSNEELRNLIKQIRNfLTQDSADLDS-IEAVANEVLKMEmpstpqqlQNLTEDIRERVESLSQVEViLQ 1562
Cdd:pfam15905 61 LKKKSQKN--LKESKDQKELEKEIRA-LVQERGEQDKrLQALEEELEKVE--------AKLNAAVREKTSLSASVAS-LE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1563 HSAADIARAEMLLE-------EAKRAS---------KSATDVKVTADMVKEalEEAEKAQVAAEKAIKQADEDIQGTQNL 1626
Cdd:pfam15905 129 KQLLELTRVNELLKakfsedgTQKKMSslsmelmklRNKLEAKMKEVMAKQ--EGMEGKLQVTQKNLEHSKGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1627 LTSIES---ETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLD---GELDEKYKK 1700
Cdd:pfam15905 207 LVSTEKekiEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSkqiKDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 167614504 1701 VENLIAKKT--EESADARRKAEMLQ-NEAKTLLAQANSKLQ 1738
Cdd:pfam15905 287 LESEKEELLreYEEKEQTLNAELEElKEKLTLEEQEHQKLQ 327
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1451-1765 |
1.26e-06 |
|
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: 53.82 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAEVEQLSKMVSEAKlradEAKQSAEdillktnATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLK 1530
Cdd:TIGR00618 168 LLMNLFPLDQYTQLALMEF----AKKKSLH-------GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1531 MEMPSTP--QQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSA---------TDVKVTADMVKEAL 1599
Cdd:TIGR00618 237 QTQQSHAylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahikavTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 E--EAEKAQVAAEKAIKQADE-DIQGTQNLLTS-----IESETAASEETLFNAsqrisELERNVEELKRKAAQnsgeAEY 1671
Cdd:TIGR00618 317 QskMRSRAKLLMKRAAHVKQQsSIEEQRRLLQTlhsqeIHIRDAHEVATSIRE-----ISCQQHTLTQHIHTL----QQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1672 IEkvvyTVKQSAEDVKKTLDgELDEKYKKVENLIAKKTEESAD--ARRKAEMLQNEAKTLLAQANSK-LQLLKDLERKYE 1748
Cdd:TIGR00618 388 KT----TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQlaHAKKQQELQQRYAELCAAAITCtAQCEKLEKIHLQ 462
|
330
....*....|....*..
gi 167614504 1749 DNQRYLEDKAQELARLE 1765
Cdd:TIGR00618 463 ESAQSLKEREQQLQTKE 479
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1472-1735 |
1.46e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1472 ADEAKQSAEDillKTNATKEKMDKSNEELRNLIKQIrnflTQDSADLDSIEAvANEVLKMEMPSTPQQLQNLTEDIRERV 1551
Cdd:COG3883 14 ADPQIQAKQK---ELSELQAELEAAQAELDALQAEL----EELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1552 ESLSQVEVILQHSAADIARAEMLLEeakraSKSATDvkvtadmvkeALEEAEkaqvAAEKAIKQADEDIQGTQNLLTSIE 1631
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLLG-----SESFSD----------FLDRLS----ALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1632 SETAASEETLFNASQRISELERNVEELKRKAAQnsgeaeyiekvvytvkqsAEDVKKTLDGELDEKYKKVENLIAKKTEE 1711
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAE------------------QEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260
....*....|....*....|....
gi 167614504 1712 SADARRKAEMLQNEAKTLLAQANS 1735
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1443-1701 |
1.59e-06 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 51.18 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1443 KAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEElrnlikqirnfLTQDSADLDSIE 1522
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEER-----------LAEALEKLEEAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1523 AVANEVLKMEmpstpQQLQNLTEDIRERVESLsqvevilqhsaadiaraEMLLEEAKRASKSA----TDVKVTADMVKEA 1598
Cdd:pfam00261 71 KAADESERGR-----KVLENRALKDEEKMEIL-----------------EAQLKEAKEIAEEAdrkyEEVARKLVVVEGD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1599 LEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIEsetaASEEtlfNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYT 1678
Cdd:pfam00261 129 LERAEERAELAESKIVELEEELKVVGNNLKSLE----ASEE---KASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQK 201
|
250 260
....*....|....*....|...
gi 167614504 1679 VKQSAEDVKKTLDGElDEKYKKV 1701
Cdd:pfam00261 202 LEKEVDRLEDELEAE-KEKYKAI 223
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
1473-1714 |
2.09e-06 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 52.87 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1473 DEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSAD-----LDSIEAVANevLKMEMPSTPQQLQNLTEDI 1547
Cdd:PTZ00341 858 NTAKNAAEQILSDEGLDEKKLKKRAESLKKLANAIEKYAGGGKKDkkakkKDAKDLSGN--IAHEINLINKELKNQNENV 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1548 RERVESLSQ------VEVILQHSAADiaRAEMLLEEAKRASKSATDVKVTADMVKEALEE--AEKAQVAAEKAIKQ-ADE 1618
Cdd:PTZ00341 936 PEHLKEHAEanieedAEENVEEDAEE--NVEENVEENVEENVEENVEENVEENVEENVEEnvEENVEENIEENVEEnVEE 1013
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQgtQNLLTSIESETAASEETLFNASQR-ISELERNVEELKRKAAQNSGEaEYIEKVVYTVKQSAED-VKKTLDGELDE 1696
Cdd:PTZ00341 1014 NIE--ENVEEYDEENVEEVEENVEEYDEEnVEEIEENAEENVEENIEENIE-EYDEENVEEIEENIEEnIEENVEENVEE 1090
|
250
....*....|....*...
gi 167614504 1697 KYKKVENLIAKKTEESAD 1714
Cdd:PTZ00341 1091 NVEEIEENVEENVEENAE 1108
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1535-1707 |
2.49e-06 |
|
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: 50.69 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1535 STPQQLQNLtEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIK 1614
Cdd:COG1579 1 AMPEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAA----------KTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1615 QADEDIQGTQNLL---------TSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAED 1685
Cdd:COG1579 70 EVEARIKKYEEQLgnvrnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|..
gi 167614504 1686 VKKTLDGELDEKYKKVENLIAK 1707
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK 171
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1458-1780 |
2.82e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1458 VEQLSKMVSEAKLRADEAKQSAEDIllktnatKEKMDKSNEELRNLIKQIRNFLTQdsadldsIEAVANEVlkmempstp 1537
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEEL-------KEKRDELNEELKELAEKRDELNAQ-------VKELREEA--------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQLQNLTEDIRERVESLSQvevilqhsaadiaRAEMLLEEAKRASKsatdvkvTADMVKEALEEAEKAQV---AAEKAIK 1614
Cdd:COG1340 60 QELREKRDELNEKVKELKE-------------ERDELNEKLNELRE-------ELDELRKELAELNKAGGsidKLRKEIE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1615 QaDEDIQGTQNLltsieseTAASEETLFnasQRISELERNVEELKRKAAQNSgeaEYIEkvvytVKQSAEDVKKTLDgEL 1694
Cdd:COG1340 120 R-LEWRQQTEVL-------SPEEEKELV---EKIKELEKELEKAKKALEKNE---KLKE-----LRAELKELRKEAE-EI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1695 DEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKD 1774
Cdd:COG1340 180 HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
....*.
gi 167614504 1775 ISQKVA 1780
Cdd:COG1340 260 KEKEEL 265
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
917-973 |
3.32e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 45.81 E-value: 3.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 917 CPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNPSEVGGSC 973
Cdd:pfam00053 1 CDCNPHGSLSDT----C--DPETGQ--CLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1440-1684 |
4.21e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 51.56 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1440 AWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNF-LTQ--DSA 1516
Cdd:COG0840 153 LAAAAAAAAALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGdLTVriDVD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1517 DLDSIEAVANEVLKMEmpstpQQLQNLTEDIRERVESLSQVEVILQHSAADIA-RAEMLLEEAKRASKSATDVKVT---- 1591
Cdd:COG0840 233 SKDEIGQLADAFNRMI-----ENLRELVGQVRESAEQVASASEELAASAEELAaGAEEQAASLEETAAAMEELSATvqev 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1592 ADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESetaaseetlfnASQRISELERNVEElkrkaaqnsgeaey 1671
Cdd:COG0840 308 AENAQQAAELAEEASELAEEGGEVVEEAVEGIEEIRESVEE-----------TAETIEELGESSQE-------------- 362
|
250
....*....|...
gi 167614504 1672 IEKVVYTVKQSAE 1684
Cdd:COG0840 363 IGEIVDVIDDIAE 375
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
867-906 |
4.52e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.99 E-value: 4.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 167614504 867 CQCN--GHADD-CDPVTGECLnCQDYTMGHNCERCLAGYYGDP 906
Cdd:smart00180 1 CDCDpgGSASGtCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1457-1774 |
4.75e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1457 EVEQLSKMVSEAKLRADEAKQSAEdillkTNATKEKMDKSNEELRNLIKQIRnflTQDSADLDSIEavanEVLKMEMPST 1536
Cdd:pfam13868 7 ELRELNSKLLAAKCNKERDAQIAE-----KKRIKAEEKEEERRLDEMMEEER---ERALEEEEEKE----EERKEERKRY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1537 PQQLQ-----NLTEDIRERVESLSQVEVILQHSAAdiARAEMLLEEAKRASKsatdVKVTADMVKEALEEAEKAQVAAEK 1611
Cdd:pfam13868 75 RQELEeqieeREQKRQEEYEEKLQEREQMDEIVER--IQEEDQAEAEEKLEK----QRQLREEIDEFNEEQAEWKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1612 AIKQADEDIQGTQNLLTSIESETAASEETLFNASQRISE--------------------LERNVEELKRKAAQNsgEAEY 1671
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArlraqqekaqdekaerdelrAKLYQEEQERKERQK--EREE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1672 IEK-------VVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTE----ESADARRKAEMLQNEAKTLLAQANSKLQL- 1739
Cdd:pfam13868 227 AEKkarqrqeLQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdeeiEQEEAEKRRMKRLEHRRELEKQIEEREEQr 306
|
330 340 350
....*....|....*....|....*....|....*
gi 167614504 1740 LKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKD 1774
Cdd:pfam13868 307 AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1437-1659 |
4.77e-06 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 50.85 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1437 AHNAWQKAMDL--DQDVLSALAEVEQ----LSKMVSEAKLraDEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNF 1510
Cdd:pfam04108 75 ALERLEETLDKlrNTPVEPALPPGEEkqktLLDFIDEDSV--EILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1511 LTQDSADLDSIeavanevlkMEMPSTPQQLQNLTEDIRERVESLS----QVEVILQHSAADiaRAEMlLEEAKRASKSAT 1586
Cdd:pfam04108 153 LESLSSPSESI---------SLIPTLLKELESLEEEMASLLESLTnhydQCVTAVKLTEGG--RAEM-LEVLENDARELD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1587 DV-----KVTADM------VKEALEEAEKAQVAAEKAIKqadeDIQGTQNLLTSIESETAASEETLFNASQRISELERNV 1655
Cdd:pfam04108 221 DVvpelqDRLDEMennyerLQKLLEQKNSLIDELLSALQ----LIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSEL 296
|
....
gi 167614504 1656 EELK 1659
Cdd:pfam04108 297 EDLR 300
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1192-1760 |
4.99e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1192 ELTNRTHRFLEKAKALKISGvigPYRETVDSVERKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKL 1271
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAA---AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1272 SDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNSD-IRGALDSitKYFQMSLEAEERVNASTTEPNSTVEQSA 1350
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADeAKKAEEA--KKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1351 LMRdRVEDVmmeRESQFKEKQEEQARlldelagklqsldlsaaaemtcgtppgascsetecggpncrtdEGERKcggpgc 1430
Cdd:PTZ00121 1550 ELK-KAEEL---KKAEEKKKAEEAKK-------------------------------------------AEEDK------ 1576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1431 gglvtvaHNAWQKAMDLDQDVLSALAEVEQLSKmvSEAKLRADEAKQSAEDillktnATKEKMDKSNEELRNLIKQIRnf 1510
Cdd:PTZ00121 1577 -------NMALRKAEEAKKAEEARIEEVMKLYE--EEKKMKAEEAKKAEEA------KIKAEELKKAEEEKKKVEQLK-- 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1511 ltqdsadldsiEAVANEVLKMEmpstpqQLQNLTEDIRERVESLSQvevilqhsaadiaRAEMLLEEAKRASKSATDVKV 1590
Cdd:PTZ00121 1640 -----------KKEAEEKKKAE------ELKKAEEENKIKAAEEAK-------------KAEEDKKKAEEAKKAEEDEKK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1591 TADMVKEALEEAEKaqvaAEKAIKQADEDIQGTQNLLTSIESETAASEetlfnasqrisELERNVEELKRKAAQ---NSG 1667
Cdd:PTZ00121 1690 AAEALKKEAEEAKK----AEELKKKEAEEKKKAEELKKAEEENKIKAE-----------EAKKEAEEDKKKAEEakkDEE 1754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1668 EAEYIEKVVYTVKQSAEDVKKTLDG----ELDEKYKKVENLIAKKTEESAD---------------ARRKAEMLQNEAKT 1728
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAvieeELDEEDEKRRMEVDKKIKDIFDnfaniieggkegnlvINDSKEMEDSAIKE 1834
|
570 580 590
....*....|....*....|....*....|...
gi 167614504 1729 LLAQANSKLQLLKDLER-KYEDNQRYLEDKAQE 1760
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKhKFNKNNENGEDGNKE 1867
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1688-1779 |
5.10e-06 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 48.68 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1688 KTLDGELDEKYKKVENLIAKKteeSADARRKAEMLQNEAKTLLAQANSKLQllKDLERKYEDNQRYLEDKAQELARLEGE 1767
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKL---EKELQALQEKLQKEAATLSEEERQKKE--RELQKKQQELQRKQQEAQQDLQKRQQE 116
|
90
....*....|..
gi 167614504 1768 vrsLLKDISQKV 1779
Cdd:COG2825 117 ---LLQPILEKI 125
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
335-387 |
6.69e-06 |
|
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: 44.65 E-value: 6.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 335 CNCNEH---SISCHFDmavylatgnvsGGVCDdCQHNTMGRNCEQCKPFYYQHPER 387
Cdd:cd00055 2 CDCNGHgslSGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1517-1743 |
7.61e-06 |
|
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: 50.23 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1517 DLDSIEAVANEvLKMEMPSTPQQLQNLTEDIRERVESLSQvevilqHSAADIARAEMLLEEAKRASKSATdvkvtADmvK 1596
Cdd:TIGR02794 44 DPGAVAQQANR-IQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQ-----AE--Q 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1597 EALEEAEKAQVAAEKAIKQADEdiqgtqnlltsiesetAASEETLFNASQRISELERNVEE--LKRKAAQNSGEAEYIEK 1674
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAE----------------AKAKAEAEAERKAKEEAAKQAEEeaKAKAAAEAKKKAEEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1675 vvytvKQSAEDVKKtldgELDEKYKKVENLIAK----KTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDL 1743
Cdd:TIGR02794 174 -----KAEAEAKAK----AEAEAKAKAEEAKAKaeaaKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDI 237
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
335-385 |
8.77e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 44.27 E-value: 8.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 335 CNCNEHSI---SCHFdmavylatgnvSGGVCDdCQHNTMGRNCEQCKPFYYQHP 385
Cdd:pfam00053 1 CDCNPHGSlsdTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLP 42
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1458-1756 |
1.20e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1458 VEQLSKMVSEAKLRADEAKqSAEDILLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADL----DSIEAVANEVLKMEM 1533
Cdd:PTZ00440 641 LDELSHFLDDHKYLYHEAK-SKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLlslkENIIKKQLNNIEQDI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1534 PSTPQQLQNLTEDIRERVESLSQVEVILQHSAADI-ARAEMLLEEAKRASKSATDVKVTADMV---KEALEEAEKA---- 1605
Cdd:PTZ00440 720 SNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIiNRKNEFILHLYENDKDLPDGKNTYEEFlqyKDTILNKENKisnd 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1606 QVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQRI---------SELERNVEELKRKAAQNSGEAEYIEKVV 1676
Cdd:PTZ00440 800 INILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFptedenlnlKELEKEFNENNQIVDNIIKDIENMNKNI 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1677 YTVKQsaedVKKTLDGELDEKyKKVENLIAKKteesADARRKAE--MLQNEAKTLLAQaNSKLQLLKDLERKYEDNQRYL 1754
Cdd:PTZ00440 880 NIIKT----LNIAINRSNSNK-QLVEHLLNNK----IDLKNKLEqhMKIINTDNIIQK-NEKLNLLNNLNKEKEKIEKQL 949
|
..
gi 167614504 1755 ED 1756
Cdd:PTZ00440 950 SD 951
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1578-1770 |
1.23e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1578 AKRASKSATDVKVTADMV----KEALEEAEKAQVAAEkaikQADEdiqgtqnlltsiESETAASEETLFNASQRISELER 1653
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTdlkeRESQEDAKRAQQLKE----ELDK------------KQIDADKAQQKADFAQDNADKQR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1654 NVEELKRKAAQNSGEAeyiekvvytVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADAR-RKAEMLQNEAKtllaq 1732
Cdd:pfam05262 248 DEVRQKQQEAKNLPKP---------ADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKdHKAFDLKQESK----- 313
|
170 180 190
....*....|....*....|....*....|....*...
gi 167614504 1733 ANSKLQllkdlERKYEDNQRYLEDKAQELARLEGEVRS 1770
Cdd:pfam05262 314 ASEKEA-----EDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1217-1385 |
1.25e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1217 RETVDSVERKVSEIKDILAQspAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNS--TAKELDSLQTEAES 1294
Cdd:COG1579 23 EHRLKELPAELAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1295 LDNTVKELAEQLefiknsdirgaldsitkyfqmsLEAEERVNASTTEPNSTVEQSALMRDRVEDVMMERESQFKEKQEEQ 1374
Cdd:COG1579 101 LKRRISDLEDEI----------------------LELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|....
gi 167614504 1375 ARLL---DELAGKL 1385
Cdd:COG1579 159 EELEaerEELAAKI 172
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
271-323 |
1.28e-05 |
|
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: 43.88 E-value: 1.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 271 CFCYGHAS---ECAPVDGfneevegmvhgHCMCRHNTKGLNCELCMDFYHDLPWRP 323
Cdd:cd00055 2 CDCNGHGSlsgQCDPGTG-----------QCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1220-1710 |
1.35e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 50.60 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1220 VDSVERKVSEIKDILAQSPAaepLKNIGNLFEEAEKLI--KDVTEMMAQVEVKLSDTT-SQSNSTA-KELDSLQTEAESL 1295
Cdd:PTZ00440 899 VEHLLNNKIDLKNKLEQHMK---IINTDNIIQKNEKLNllNNLNKEKEKIEKQLSDTKiNNLKMQIeKTLEYYDKSKENI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1296 DNTVKELAEQLEFIKNS--DIRGALDSITKYFQMsleAEERVNasttepNSTVEQSALMRDRVEDVMMERESQFKEKQEE 1373
Cdd:PTZ00440 976 NGNDGTHLEKLDKEKDEweHFKSEIDKLNVNYNI---LNKKID------DLIKKQHDDIIELIDKLIKEKGKEIEEKVDQ 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1374 QARLLDELAGKLQSLDLSAAAEMTCGTPPGASCSETEcggpncrtdegerkcggpgcgglvtvahnawQKAMDLDQDVLS 1453
Cdd:PTZ00440 1047 YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLE-------------------------------EKVEALLKKIDE 1095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1454 ALAEVEQLSKMVSEAKLRAD-EAKQSAEDIllktNATKEKMDKSNEELRNLIKQIRNfltqdsadLDSIEAVANEVLKME 1532
Cdd:PTZ00440 1096 NKNKLIEIKNKSHEHVVNADkEKNKQTEHY----NKKKKSLEKIYKQMEKTLKELEN--------MNLEDITLNEVNEIE 1163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1533 MP-------STPQQLQNLTED---IRERVES------LSQVEVI--------------LQHSAAD--------IARAEML 1574
Cdd:PTZ00440 1164 IEyerilidHIVEQINNEAKKsktIMEEIESykkdidQVKKNMSkerndhlttfeynaYYDKATAsyenieelTTEAKGL 1243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1575 LEEAKRaSKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQadedIQGTQNLLTSIESETAASEetLFNASQRISELERN 1654
Cdd:PTZ00440 1244 KGEANR-STNVDELKEIKLQVFSYLQQVIKENNKMENALHE----IKNMYEFLISIDSEKILKE--ILNSTKKAEEFSND 1316
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1655 VE-ELKRkaaqnsgEAEYIEKVVYTVKQSAEDVKKTL----DGELDEKYKKV----ENLIAKKTE 1710
Cdd:PTZ00440 1317 AKkELEK-------TDNLIKQVEAKIEQAKEHKNKIYgsleDKQIDDEIKKIeqikEEISNKRKE 1374
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1457-1767 |
1.37e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.03 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1457 EVEQLSKMVSEAKLRADEAKQSAEDIL------------LKTN---ATKEKMD-KSNEELRNLIKQIrnfLTQDSADLDS 1520
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEAAKAQVLeelestkrlieeLKLNlerAQTEEAQaKQDSELAKLRVEE---MEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1521 IEAVAN-EVLKMEMPSTPQQLQNltedIRERVESLSQVEVILQhSAADIA--RAEMLLEEAKRASKSATDVKVTADMVKE 1597
Cdd:pfam05701 120 VAAKAQlEVAKARHAAAVAELKS----VKEELESLRKEYASLV-SERDIAikRAEEAVSASKEIEKTVEELTIELIATKE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1598 ALE-------EAEKAQVAA-----------EKAIKQADEDIQGTQNLLTS---IESETAASEETLFNASqriSELERNVE 1656
Cdd:pfam05701 195 SLEsahaahlEAEEHRIGAalareqdklnwEKELKQAEEELQRLNQQLLSakdLKSKLETASALLLDLK---AELAAYME 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1657 -ELKRKAAQNSGEAEY---IEKVVYTVKQSAEDVKKTLDGELDE-KYKKV--ENL---IAKKTEESADARRKAEMLQNEA 1726
Cdd:pfam05701 272 sKLKEEADGEGNEKKTstsIQAALASAKKELEEVKANIEKAKDEvNCLRVaaASLrseLEKEKAELASLRQREGMASIAV 351
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 167614504 1727 KTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQEL--ARLEGE 1767
Cdd:pfam05701 352 SSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLqqAAQEAE 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1442-1686 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1442 QKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRnfltQDSADLDSI 1521
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY----RSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1522 EAVANevlkmempSTpqqlqNLTEDIrERVESLSQV----EVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKE 1597
Cdd:COG3883 106 DVLLG--------SE-----SFSDFL-DRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1598 ALEEAEKAQvaaEKAIKQADEDIQGTQNLLTSIESETAASEETLfNASQRISELERNVEELKRKAAQNSGEAEYIEKVVY 1677
Cdd:COG3883 172 ELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAA-AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*....
gi 167614504 1678 TVKQSAEDV 1686
Cdd:COG3883 248 GAGAAGAAG 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1572-1771 |
1.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1572 EMLLEEakrasksaTDVKVTADMVKEALEEAEKAQVAAEKAIKQAdediqgtqnlltsiesetaaseETLfnasQRISEL 1651
Cdd:COG4913 215 EYMLEE--------PDTFEAADALVEHFDDLERAHEALEDAREQI----------------------ELL----EPIREL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1652 ERNVEELKRKAAQNSGEAEYIEkvVYTVKQSAEDVKKTLDgELDEKYKKVENLIAKKTEESADARRKAEMLQNeaktllA 1731
Cdd:COG4913 261 AERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELE-ELRAELARLEAELERLEARLDALREELDELEA------Q 331
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167614504 1732 QANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSL 1771
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1617-1782 |
1.99e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1617 DEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEyiekvvyTVKQSAEDVKKTLDG---- 1692
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1693 -ELDEKYKKVENLiAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLK-DLERKYEDNQRYLEDKAQELARLEGEVRS 1770
Cdd:COG1579 89 kEYEALQKEIESL-KRRISDLEDEILELMERIEELEEELAELEAELAELEaELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|...
gi 167614504 1771 LLKDISQK-VAVY 1782
Cdd:COG1579 168 LAAKIPPElLALY 180
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1693-1780 |
2.51e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 45.65 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1693 ELDEKYKKVENLIAKKteeSADARRKAEMLQNEAKTLLAQANSKLQllKDLERKYEDNQRYLEDKAQELARLEGE----V 1768
Cdd:smart00935 22 QLEKEFKKRQAELEKL---EKELQKLKEKLQKDAATLSEAAREKKE--KELQKKVQEFQRKQQKLQQDLQKRQQEelqkI 96
|
90
....*....|..
gi 167614504 1769 RSLLKDISQKVA 1780
Cdd:smart00935 97 LDKINKAIKEVA 108
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1575-1778 |
2.54e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1575 LEEAKRASKSATD---VKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQnlltsiESETAASEETlfnaSQRISEL 1651
Cdd:pfam07888 9 LEEESHGEEGGTDmllVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEK------ERYKRDREQW----ERQRREL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1652 ERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEK------YKKVENLIAKKTEESADARRKAEMLQNE 1725
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRaahearIRELEEDIKTLTQRVLERETELERMKER 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 167614504 1726 AKTLLAQansklqlLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:pfam07888 159 AKKAGAQ-------RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQR 204
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1564-1710 |
2.78e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 48.71 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1564 SAADIARAEMLLEEAKRASKSATDVKVTADM-------VKEALEEAEKAQVAAEKAIKQADEDIQGTQNlltsiESETAA 1636
Cdd:PRK12472 185 LAAAPARAETLAREAEDAARAADEAKTAAAAaareaapLKASLRKLERAKARADAELKRADKALAAAKT-----DEAKAR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1637 SEETLFNASQRISELERNVE------ELKRKAAQNSGEAeyiEKVVYTVKqsAEDVKKTLDGELdeKYKKVENLIAKKTE 1710
Cdd:PRK12472 260 AEERQQKAAQQAAEAATQLDtakadaEAKRAAAAATKEA---AKAAAAKK--AETAKAATDAKL--ALEPVSIYISRATQ 332
|
|
| GARP |
pfam16731 |
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, ... |
1570-1731 |
2.96e-05 |
|
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, is one of a subset of major surface molecules on Trypanosoma species. They are all surface-orientated, immunodominant, and highly charged. GARP is interesting as ts expression coincides with the loss and gain of variant surface glycoprotein (VSG) molecules in the tsetse vector. It has an extended helical bundle structure that is homologous to the core surface structure of VSG, suggesting that it might replace the bloodstream VSG as the trypanosomes differentiate inside the tsetse vector after a blood-meal.
Pssm-ID: 435545 [Multi-domain] Cd Length: 192 Bit Score: 46.60 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1570 RAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKqadeDIQGTQNLLTSIESETAASEETLFnasQRIS 1649
Cdd:pfam16731 40 QAEEAVELAESAGLNDPKAKEAVTRAREAAVRATEAAEAAATAAS----NVEINAANLASVAWAYVPSLDDGL---KKLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1650 ELERNVEELKRKAAQNSGEAEyiekvVYTVK---QSAEDVKKTLDGELDEKYKKvenliakkteESADARRKAEMLQNEA 1726
Cdd:pfam16731 113 ECGNADEDVREAAKKCTKTAE-----NVTAQsltEALEGLRKLFDVKSAERLRK----------ETVEAHEELKSLEKAV 177
|
....*
gi 167614504 1727 KTLLA 1731
Cdd:pfam16731 178 EEAVR 182
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
916-974 |
3.13e-05 |
|
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: 42.73 E-value: 3.13e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 916 PCPCPDGPDSGRQfarsCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNPSeVGGSCQ 974
Cdd:cd00055 1 PCDCNGHGSLSGQ----C--DPGTGQ--CECKPNTTGRRCDRCAPGYYGLPS-QGGGCQ 50
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1235-1389 |
4.45e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1235 AQSPAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEvklsDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQL-------- 1306
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELE----ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeerreelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1307 EFIKNSDIRGALDSitkYFQMSLEAE------ERVNASTTEP---NSTVEQSALMRDRVEdvmmERESQFKEKQEEQARL 1377
Cdd:COG3883 90 ERARALYRSGGSVS---YLDVLLGSEsfsdflDRLSALSKIAdadADLLEELKADKAELE----AKKAELEAKLAELEAL 162
|
170
....*....|..
gi 167614504 1378 LDELAGKLQSLD 1389
Cdd:COG3883 163 KAELEAAKAELE 174
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1576-1729 |
5.19e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1576 EEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLfnASQRISELERNV 1655
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQV--AENQKREIEKAQ 287
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1656 EELKRKAaqnsgeaeyiEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTL 1729
Cdd:pfam05262 288 IEIKKND----------EEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1491-1779 |
5.45e-05 |
|
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: 47.02 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1491 EKMDKSNEELRNLIKQIRNFLTQDSADLDSIEavaneVLKmempstpQQLQNLTEDIRERVESLSQVevilqhsaadIAR 1570
Cdd:pfam06008 12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIE-----ILE-------KELSSLAQETEELQKKATQT----------LAK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1571 AEMLLEEAKRASKSAtdvkvtadmvKEALEEAEKAQVAAEKAIKQAdediqgtqnlLTSIESETAASEETLFNASQrisE 1650
Cdd:pfam06008 70 AQQVNAESERTLGHA----------KELAEAIKNLIDNIKEINEKV----------ATLGENDFALPSSDLSRMLA---E 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1651 LERNVEELKRKAAQnsgeaeyiekvvyTVKQSAEDVKKtldgELDEKYKKVENLIAKKTEESadarrkaEMLQNEAKTLL 1730
Cdd:pfam06008 127 AQRMLGEIRSRDFG-------------TQLQNAEAELK----AAQDLLSRIQTWFQSPQEEN-------KALANALRDSL 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 167614504 1731 AQANSKLQLLKDLERKyednqryLEDKAQELARLEGEVRSLLKDISQKV 1779
Cdd:pfam06008 183 AEYEAKLSDLRELLRE-------AAAKTRDANRLNLANQANLREFQRKK 224
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1569-1737 |
5.51e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 47.94 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1569 ARAEMLLEEAKRASKSatdvkVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLT--------------SIESET 1634
Cdd:PRK00106 53 RDAEHIKKTAKRESKA-----LKKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTeratsldrkdenlsSKEKTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1635 AASEETLFNASQRISELERNVEELKRKaaqnsgEAEYIEKVVYTVKQSAEDVKktldgeLDEKYKKVENLIAKKTEESad 1714
Cdd:PRK00106 128 ESKEQSLTDKSKHIDEREEQVEKLEEQ------KKAELERVAALSQAEAREII------LAETENKLTHEIATRIREA-- 193
|
170 180
....*....|....*....|...
gi 167614504 1715 ARRKAEMLQNEAKTLLAQANSKL 1737
Cdd:PRK00106 194 EREVKDRSDKMAKDLLAQAMQRL 216
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1451-1742 |
6.70e-05 |
|
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: 47.91 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1451 VLSALAEVEQLSKMVSEAKLR-ADEAKQSAE-------DILLKTNATKEKMDKSNEELrnliKQIRNFLTQDSADLDSIE 1522
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLiASRQEERQEtsaelnqLLRTLDDQWKEKRDELNGEL----SAADAAVAKDRSELEALE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1523 AVANEVLKMEMPSTPQQLQNLtEDIRERVESLSQVEVILQHSAADIARAEMLLEeAKRASKSATDVKVTADMVKEALEEA 1602
Cdd:pfam12128 329 DQHGAFLDADIETAAADQEQL-PSWQSELENLEERLKALTGKHQDVTAKYNRRR-SKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1603 EKaQVAAEKAIKQADE----DIQGTQNLLTSIESE---------------TAASEETLFNASQRISELERNVEEL-KRKA 1662
Cdd:pfam12128 407 DR-QLAVAEDDLQALEselrEQLEAGKLEFNEEEYrlksrlgelklrlnqATATPELLLQLENFDERIERAREEQeAANA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1663 AQNSGeaeyiekvvytvkQSAEDVKKTLDGELDEKYkkveNLIAKKTEESADARRKAE-MLQNEAKTLLAQANSKLQLLK 1741
Cdd:pfam12128 486 EVERL-------------QSELRQARKRRDQASEAL----RQASRRLEERQSALDELElQLFPQAGTLLHFLRKEAPDWE 548
|
.
gi 167614504 1742 D 1742
Cdd:pfam12128 549 Q 549
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1540-1771 |
6.86e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1540 LQN-LTEDIRERVEslsqvevILQHSAADIARAEMLLEEAKRAsKSATDVKVTAdmVKEALEEAEKAQVAAEKAIKQADE 1618
Cdd:pfam07888 32 LQNrLEECLQERAE-------LLQAQEAANRQREKEKERYKRD-REQWERQRRE--LESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNsgEAEyIEKVVYTVKQSAedvkktldGELDEKY 1698
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLER--ETE-LERMKERAKKAG--------AQRKEEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 1699 KKVENLIAKKTEESADARRKAEMLQnEAKTLLAQANSKLQLLKD----LERKYEDNQRyledKAQELARLEGEVRSL 1771
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSLSKEFQ-ELRNSLAQRDTQVLQLQDtittLTQKLTTAHR----KEAENEALLEELRSL 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1570-1733 |
6.86e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1570 RAEMLLEEAKRASKSATDVKVTadmvkEALEEAEKAQVAAEKAIKQADEDIQGTQN--------------LLTSIESETA 1635
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALL-----EAKEEIHKLRNEFEKELRERRNELQKLEKrllqkeenldrkleLLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1636 ASEETLFNASQRISELERNVEELKRKAAQnsgEAEYIEKVvytvkqSAEDVKKTLDGELDEKYKKVENLIAKKTEEsaDA 1715
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQ---ELERISGL------TAEEAKEILLEKVEEEARHEAAVLIKEIEE--EA 182
|
170
....*....|....*...
gi 167614504 1716 RRKAEMlqnEAKTLLAQA 1733
Cdd:PRK12704 183 KEEADK---KAKEILAQA 197
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1539-1743 |
6.98e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1539 QLQNLTEDIRERVESLSQVEVilQHSAADIARAEMLLEEAKRAsKSATDVKVTADMVKEALEEAekAQVAAEKAIKQADE 1618
Cdd:PRK09510 99 EQERLKQLEKERLAAQEQKKQ--AEEAAKQAALKQKQAEEAAA-KAAAAAKAKAEAEAKRAAAA--AKKAAAEAKKKAEA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1619 DIQGTQNLLTSIESETAASEETlfnasqriselernVEELKRKAAQnsgEAEyiekvvytvKQSAEDVKKTLDGELDEKY 1698
Cdd:PRK09510 174 EAAKKAAAEAKKKAEAEAAAKA--------------AAEAKKKAEA---EAK---------KKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167614504 1699 KKVEnliakkteesADARRKAEMLQNEAKTLLAQANSKLQLLKDL 1743
Cdd:PRK09510 228 AKAA----------AEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
1569-1733 |
7.96e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 45.65 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1569 ARAEMLLEEAKrasKSATDVKvtadmvKEAL----EEAEKAQVAAEKAIKQADEDIQGTQN--------------LLTSI 1630
Cdd:pfam12072 34 ELAKRIIEEAK---KEAETKK------KEALleakEEIHKLRAEAERELKERRNELQRQERrllqkeetldrkdeSLEKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1631 ESETAASEETLFNASQRISELERNVEELKRKAAQnsgEAEYIEKVvytvkqSAEDVKKTLdgeLDEKYKKVENLIAKKTE 1710
Cdd:pfam12072 105 EESLEKKEKELEAQQQQLEEKEEELEELIEEQRQ---ELERISGL------TSEEAKEIL---LDEVEEELRHEAAVMIK 172
|
170 180
....*....|....*....|....
gi 167614504 1711 ES-ADARRKAEmlqNEAKTLLAQA 1733
Cdd:pfam12072 173 EIeEEAKEEAD---KKAKEIIALA 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1257-1611 |
8.82e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1257 IKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKN--SDIRGALDSITKYFQMSleAEER 1334
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREeaQELREKRDELNEKVKEL--KEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1335 vnasttepNSTVEQSALMRDRVEDVMMERESQFKEKQEEQA--RLLDELAGKLQSLDLSAAAEMTcgtppgascsetecg 1412
Cdd:COG1340 81 --------DELNEKLNELREELDELRKELAELNKAGGSIDKlrKEIERLEWRQQTEVLSPEEEKE--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1413 gpncrtdegerkcggpgcggLV-TVAH-----NAWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKT 1486
Cdd:COG1340 138 --------------------LVeKIKElekelEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1487 NATKEKMDKSNEELRNLIKQIRNFltqdSADLDSIEavanevlkmempstpQQLQNLTEDIRErveslsqvevilqhsaa 1566
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEA----QEKADELH---------------EEIIELQKELRE----------------- 241
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 167614504 1567 diaraemLLEEAKRASKSATDVKVTADmvKEALEeaEKAQVAAEK 1611
Cdd:COG1340 242 -------LRKELKKLRKKQRALKREKE--KEELE--EKAEEIFEK 275
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1621 |
9.44e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1247 GNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEfiknsdirgaldsitkyfq 1326
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1327 mslEAEERVNASTTEPNSTVEQSALMRDRVEdvmmERESQFKEKQEEQARL---LDELAGKLQSLDlsaaaemtcgtppg 1403
Cdd:COG4372 84 ---ELNEQLQAAQAELAQAQEELESLQEEAE----ELQEELEELQKERQDLeqqRKQLEAQIAELQ-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1404 ascsetecggpncrTDEGERKcggpgcgglvtvahnawQKAMDLDQDVLSALAEVEQLSKmvSEAKLRADEAKQSAEDIL 1483
Cdd:COG4372 143 --------------SEIAERE-----------------EELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1484 LKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQH 1563
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1564 SAADIARAEMLLEEAKRASKSATDVK--VTADMVKEALEEAEKAQVAAEKAIKQADEDIQ 1621
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELklLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1440-1712 |
9.86e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1440 AWQKAMDLDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDIllktNATKEKMDKSNEELRNLIKQIRNFLTQDSADLD 1519
Cdd:COG4372 78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 S-----------IEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDV 1588
Cdd:COG4372 154 EleeqleslqeeLAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1589 KVTADMVKEALEEAEKAQ--VAAEKAIKQADEDIQGTQNLLTSIES--ETAASEETLFNASQRISELERNVEELKRKAAQ 1664
Cdd:COG4372 234 ALSALLDALELEEDKEELleEVILKEIEELELAILVEKDTEEEELEiaALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 167614504 1665 NSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEES 1712
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSK 361
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1567-1783 |
1.03e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1567 DIARAEMLLEEAK----RASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLF 1642
Cdd:pfam02463 168 KRKKKEALKKLIEetenLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1643 NASQRISELERNVEELKRKAAQNSGEAEYIEKVvytvKQSAEDVKKTLDGELDEKYKKVENLI-AKKTEESADARRKAEM 1721
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE----KKLQEEELKLLAKEEEELKSELLKLErRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1722 LQNEAKTLLAQANS--KLQLLKDLERKYEDNqrylEDKAQELARLEGEVRSLLKDISQKVAVYS 1783
Cdd:pfam02463 324 KKAEKELKKEKEEIeeLEKELKELEIKREAE----EEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1688-1779 |
1.04e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 44.10 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1688 KTLDGELDEKYKKVENLIAKKTEEsadARRKAEMLQNEAKTLLAQansKLQLLKDLERKYEDNQRYLEDKAQELARLEGE 1767
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKE---LQKLYEELQKDGALLEEE---REEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
|
90
....*....|..
gi 167614504 1768 vrsLLKDISQKV 1779
Cdd:pfam03938 92 ---LLQPIQDKI 100
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1221-1395 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1221 DSVERKVSEIKDILAQSPAAEplKNIGNLFEEAEKLIKDVtemmAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVK 1300
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQ--AELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1301 ELAEQL--------------------EFIKNSDirgALDSITKYFQMSLE----AEERVNASTTEPNSTVEQSALMRDRV 1356
Cdd:COG3883 90 ERARALyrsggsvsyldvllgsesfsDFLDRLS---ALSKIADADADLLEelkaDKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167614504 1357 EDVMMERESQFKEKQEEQARL---LDELAGKLQSLDLSAAAE 1395
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLsaeEAAAEAQLAELEAELAAA 208
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1192-1382 |
1.11e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1192 ELTNRTHRFLEKAKALK-ISGVIGPYRETVDSVERKVSEIKDILaQSpaaEPLKnignlFEEAEKLIKDVTEMMAQVEV- 1269
Cdd:COG1340 82 ELNEKLNELREELDELRkELAELNKAGGSIDKLRKEIERLEWRQ-QT---EVLS-----PEEEKELVEKIKELEKELEKa 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1270 -KLSDTTSQSNSTAKELDSLQTEAESLDNTVKELAEQLEFIKNS--DIRGALDSITK----YFQMSLEAEERVNASTTEP 1342
Cdd:COG1340 153 kKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmiELYKEADELRKeadeLHKEIVEAQEKADELHEEI 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167614504 1343 NSTVEQsalMRDRVEDVMMERESQFKEKQEEQARLLDELA 1382
Cdd:COG1340 233 IELQKE---LRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1476-1778 |
1.11e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 47.52 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1476 KQSAEDIL-LKTNATKEKMDKSneELRNLIKQIRNFLTQDSADLDSIEAVANEVLKME--MPSTpqqLQNLTEDIRERVE 1552
Cdd:PTZ00440 319 EKGKEYIKrIQNNNIPPQVKKD--ELKKKYFESAKHYASFKFSLEMLSMLDSLLIKKEkiLNNL---FNKLFGDLKEKIE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1553 SLSQVEVILQHSAADIARAEMLLEEAKRASKSAT---------------DVKVTADMVKEALEEA--------------- 1602
Cdd:PTZ00440 394 TLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSqkiadyalysnleiiEIKKKYDEKINELKKSinqlktlisimksfy 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1603 -----EKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLFNASQR---------------------ISELERNVE 1656
Cdd:PTZ00440 474 dliisEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNiedyyitieglkneieglielIKYYLQSIE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1657 ELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKK--TLDGELDEKYKKVENLIAKKTEESADARRKAEMLQNEAKTLLAQ-- 1732
Cdd:PTZ00440 554 TLIKDEKLKRSMKNDIKNKIKYIEENVDHIKDiiSLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKfy 633
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 167614504 1733 ANSKLQLLKDLERKYEDNQRYLEDkaqelARLEGEVRSLLKDISQK 1778
Cdd:PTZ00440 634 KGDLQELLDELSHFLDDHKYLYHE-----AKSKEDLQTLLNTSKNE 674
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
1474-1634 |
1.20e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 44.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1474 EAKQSAEDILLKTNATKEKM--DKSNEELRNLIK-QIRNFLTQDSADLDSI--EAV-ANEVLKMEMPSTPQQLQNLTEDI 1547
Cdd:cd13769 5 ELIQKAQEAINNLAQQVQKQlgLQNPEEVVNTLKeQSDNFANNLQEVSSSLkeEAKkKQGEVEEAWNEFKTKLSETVPEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1548 RERVESLSQVEVILQHSAADIaraEMLLEEAKrasKSATDVKvtadmvkealEEAEKAQVAAEKAIKQA-DEDIQGTQNL 1626
Cdd:cd13769 85 RKSLPVEEKAQELQAKLQSGL---QTLVTESQ---KLAKAIS----------ENSQKAQEELQKATKQAyDIAVEAAQNL 148
|
....*...
gi 167614504 1627 LTSIESET 1634
Cdd:cd13769 149 QNQLQTAT 156
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1595-1769 |
1.24e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1595 VKEALEEAEKAQVAAEKAIKqaDEDIQGTQnlltsiesetaaseETLFNASQRISELERN---VEELKRKAAQNSGEAEY 1671
Cdd:PTZ00121 1029 IEELTEYGNNDDVLKEKDII--DEDIDGNH--------------EGKAEAKAHVGQDEGLkpsYKDFDFDAKEDNRADEA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1672 IEKVvytvKQSAEDVKKTLDGELDEKYKKVENLiaKKTEES--ADARRKAEMLQNEAKTLLAQANSKLQLLKDLE--RKY 1747
Cdd:PTZ00121 1093 TEEA----FGKAEEAKKTETGKAEEARKAEEAK--KKAEDArkAEEARKAEDARKAEEARKAEDAKRVEIARKAEdaRKA 1166
|
170 180
....*....|....*....|..
gi 167614504 1748 EDNQRYLEDKAQELARLEGEVR 1769
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVR 1188
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
976-1019 |
1.31e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.14 E-value: 1.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 167614504 976 CQCHNniDTTDPEACDKETGRCLkCLYHTEGEHCQFCRFGYYGD 1019
Cdd:smart00180 1 CDCDP--GGSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
335-388 |
1.80e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 40.76 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 335 CNCNE---HSISCHFDmavylatgnvsGGVCDdCQHNTMGRNCEQCKPFYYQHPERD 388
Cdd:smart00180 1 CDCDPggsASGTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1574-1769 |
1.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1574 LLEEAKrasKSATDVKVTADMVKEALEEAEKAQVAAEkaIKQADEdiqgtqnlLTSIESETAASEETLFNASQRISELER 1653
Cdd:PTZ00121 1099 KAEEAK---KTETGKAEEARKAEEAKKKAEDARKAEE--ARKAED--------ARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1654 NVEELKRKAAQNSGEAEYIEKVVYTVK-QSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQN---EAKTL 1729
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEElRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKdaeEAKKA 1245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 167614504 1730 LAQANSKLQLLKDLERKYEDNQRYLEDKAQElARLEGEVR 1769
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELK 1284
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1569-1777 |
2.03e-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: 46.60 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1569 ARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEK--AIKQADEDIQGTQnLLTSIEsetaASEETLFNASQ 1646
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYE-LLKEKE----ALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1647 RISELERNVEELKRKAAQNSGEAEYIEKVvytvkqsaedvkktldgeLDEKYKKVEnliaKKTEESadarrkaemlQNEA 1726
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQL------------------LEELNKKIK----DLGEEE----------QLRV 292
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167614504 1727 KTLLAQANSKLQLLkdlERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQ 1777
Cdd:TIGR02169 293 KEKIGELEAEIASL---ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1439-1630 |
2.11e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 46.01 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1439 NAWQKAMDL------DQDVLSALAEVEQLS---KMVSEAKlraDEAKQSAEDIllktnatkEKMDKSNeelRNLIKQIRN 1509
Cdd:PRK00106 39 NAEQEAVNLrgkaerDAEHIKKTAKRESKAlkkELLLEAK---EEARKYREEI--------EQEFKSE---RQELKQIES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1510 FLTQDSADLD-SIEAVANEVLKMEmpSTPQQLQNLTEDIRERVESLSQVEvilQHSAADIAR-AEMLLEEAKRASKSATD 1587
Cdd:PRK00106 105 RLTERATSLDrKDENLSSKEKTLE--SKEQSLTDKSKHIDEREEQVEKLE---EQKKAELERvAALSQAEAREIILAETE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1588 VKVTADM---VKEALEEA-EKAQVAAEKAIKQADEDIQG---TQNLLTSI 1630
Cdd:PRK00106 180 NKLTHEIatrIREAEREVkDRSDKMAKDLLAQAMQRLAGeyvTEQTITTV 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1183-1767 |
2.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1183 FALWDVIIAELT--NRTHRFLEKAKA-LKISGVIGPYRETVDSVERKVSEIKDILAQSPAAEPLKNIgnlfEEAEKLIKD 1259
Cdd:COG4913 224 FEAADALVEHFDdlERAHEALEDAREqIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL----ELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1260 VTEMMAQVEVKLSDTTSQSNSTAKELDSLQTEAESLD-NTVKELAEQLEFIKN-----SDIRGALDSITKYFQMSLEAEE 1333
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLEReleerERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1334 RVNAST-TEPNSTVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDELAG----------KLQSL--DLSAAAEMTCGT 1400
Cdd:COG4913 380 EEFAALrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnipaRLLALrdALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1401 PPGAscsetecggpncrtdeGErkcggpgcggLVTVA--HNAWQKAM---------DL--DQDVLSALAE-VEQLSKmvs 1466
Cdd:COG4913 460 LPFV----------------GE----------LIEVRpeEERWRGAIervlggfalTLlvPPEHYAAALRwVNRLHL--- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1467 EAKLRADEAKQSAEDILLKT---NATKEKMD-KSNE---ELRNLIKQIRNFLTQDSadldsieavanevlkmempstPQQ 1539
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRldpDSLAGKLDfKPHPfraWLEAELGRRFDYVCVDS---------------------PEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1540 LQN----LTE-------------DIRERVESLSqvevILQHSAAD-----IARAEMLLEEAKRASKSATDVKVTADMVKE 1597
Cdd:COG4913 570 LRRhpraITRagqvkgngtrhekDDRRRIRSRY----VLGFDNRAklaalEAELAELEEELAEAEERLEALEAELDALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1598 ALEEAEKAQVA--AEKAIKQADEDIQGTQNLLTSIEsetaASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKV 1675
Cdd:COG4913 646 RREALQRLAEYswDEIDVASAEREIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1676 VytvkQSAEDVKKTLDGELDEkykkVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYED------ 1749
Cdd:COG4913 722 L----EQAEEELDELQDRLEA----AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEeleram 793
|
650 660 670
....*....|....*....|....*....|....
gi 167614504 1750 ---NQRY-------------LEDKAQELARLEGE 1767
Cdd:COG4913 794 rafNREWpaetadldadlesLPEYLALLDRLEED 827
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1539-1767 |
2.58e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 44.27 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1539 QLQNLTEDIRERVESL-SQV--EVILQHSaadIARAEMLLEEAKRasksatdvkvtadMVKEALEEAEKAQVAAEkaikq 1615
Cdd:pfam15665 26 EIQQILAETREKILQYkSKIgeELDLKRR---IQTLEESLEQHER-------------MKRQALTEFEQYKRRVE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1616 adediqgtqnlltsiESETAASEEtlfnASQRISELERNVEELKRKAaqnsgeAEYIEKVVYTVKQSAEDVKKTLDgELD 1695
Cdd:pfam15665 85 ---------------ERELKAEAE----HRQRVVELSREVEEAKRAF------EEKLESFEQLQAQFEQEKRKALE-ELR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167614504 1696 EKYKK-VENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKdLERK--YEDNQRYLEdKAQELARLEGE 1767
Cdd:pfam15665 139 AKHRQeIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKEVEDLR-KEKKklAEEYEQKLS-KAQAFYERELE 211
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1574-1766 |
3.01e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1574 LLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEkaikqADEDIQGTQNLLTSIESETAASEEtlfnASQRISELER 1653
Cdd:COG0497 170 LKKELEELRADEAERARELDLLRFQLEELEAAALQPG-----EEEELEEERRRLSNAEKLREALQE----ALEALSGGEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1654 NVEELKRKAAQNsgeaeyIEKVVytvkqsaedvkkTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQ-NEAKtlLAQ 1732
Cdd:COG0497 241 GALDLLGQALRA------LERLA------------EYDPSLAELAERLESALIELEEAASELRRYLDSLEfDPER--LEE 300
|
170 180 190
....*....|....*....|....*....|....*...
gi 167614504 1733 ANSKLQLLKDLERKY----EDNQRYLEDKAQELARLEG 1766
Cdd:COG0497 301 VEERLALLRRLARKYgvtvEELLAYAEELRAELAELEN 338
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1644-1772 |
3.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1644 ASQRISELERNVEELKrKAAQNsgEAEYIEK-VVYTVKQSAEDVKKTLDGELDEK---YKKVENLIAKKtEESADarRKA 1719
Cdd:PRK12704 29 AEAKIKEAEEEAKRIL-EEAKK--EAEAIKKeALLEAKEEIHKLRNEFEKELRERrneLQKLEKRLLQK-EENLD--RKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 167614504 1720 EMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEG----EVRSLL 1772
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGltaeEAKEIL 159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1439-1778 |
3.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1439 NAWQKAmDLDQDVLSALAEVEQLSKMVSEAK--LRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNfLTQDSA 1516
Cdd:COG4913 608 NRAKLA-ALEAELAELEEELAEAEERLEALEaeLDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1517 DLDSIEAVANEvLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRAS-----KSATDVKVT 1591
Cdd:COG4913 686 DLAALEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfAAALGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1592 ADM-------VKEALEEAEKAQVAAEKAIKQADED-IQGTQNLLTSIESETAASEEtlfNASQRISELERNVEELKRKAA 1663
Cdd:COG4913 765 RELrenleerIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL---LDRLEEDGLPEYEERFKELLN 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1664 QNSGEAeyIEKVVYTVKQSAEDVKKTLD---GEL-------DEKYKkvenlIAKKTEESADARRKAEMLQ--NEAKTL-- 1729
Cdd:COG4913 842 ENSIEF--VADLLSKLRRAIREIKERIDplnDSLkripfgpGRYLR-----LEARPRPDPEVREFRQELRavTSGASLfd 914
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1730 LAQANSKLQLLKDL-ER--------------KYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:COG4913 915 EELSEARFAALKRLiERlrseeeesdrrwraRVLDVRNHLEFDAEEIDREDGEEVETYSSSGGK 978
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1565-1707 |
4.31e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.47 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1565 AADIARAEMLLEEAKRASKSAT----DVKVTAD-MVKEALEEAEKaqvAAEKAIKQADEDiqgtqnlltsIESETAASEE 1639
Cdd:COG0711 37 ADGLAEAERAKEEAEAALAEYEeklaEARAEAAeIIAEARKEAEA---IAEEAKAEAEAE----------AERIIAQAEA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1640 TLfnasqrisELERN--VEELKRKAAQNSGEAeyIEKVvytvkqsaedVKKTLDGELDEKYkkVENLIAK 1707
Cdd:COG0711 104 EI--------EQERAkaLAELRAEVADLAVAI--AEKI----------LGKELDAAAQAAL--VDRFIAE 151
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1433-1662 |
4.40e-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: 44.28 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1433 LVTVAHNAWQKAMDLDQDVLSALAEVEQLSKMVSEA--KLRADEAKQSAEDILlktNATKEKMDKSNEELRNLIKQIRNF 1510
Cdd:cd22656 71 IVSLAGDIYNYAQNAGGTIDSYYAEILELIDDLADAtdDEELEEAKKTIKALL---DDLLKEAKKYQDKAAKVVDKLTDF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1511 LTQ---DSADLDSIEAVANEVLKMEMPSTPQ-QLQNLTEDI--------RERVESLSQVEVILQHSAADIARAEMLLEEA 1578
Cdd:cd22656 148 ENQtekDQTALETLEKALKDLLTDEGGAIARkEIKDLQKELeklneeyaAKLKAKIDELKALIADDEAKLAAALRLIADL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1579 KRASKSATDVKvtaDMVKEALEEAEKAQVAAEkAIKQadeDIQGTQNLLTSIESETAASeetlFNASQRISELERNVEEL 1658
Cdd:cd22656 228 TAADTDLDNLL---ALIGPAIPALEKLQGAWQ-AIAT---DLDSLKDLLEDDISKIPAA----ILAKLELEKAIEKWNEL 296
|
....
gi 167614504 1659 KRKA 1662
Cdd:cd22656 297 AEKA 300
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1630-1764 |
4.43e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1630 IESETAASEETLFNASQRISELERNVE---ELKRKAAQNSGEAeYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIA 1706
Cdd:PRK00106 26 MKSAKEAAELTLLNAEQEAVNLRGKAErdaEHIKKTAKRESKA-LKKELLLEAKEEARKYREEIEQEFKSERQELKQIES 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167614504 1707 KKTEESADARRKAEMLQNEAKTLlaqaNSKLQLLKDLERKYEDNQRYL----EDKAQELARL 1764
Cdd:PRK00106 105 RLTERATSLDRKDENLSSKEKTL----ESKEQSLTDKSKHIDEREEQVekleEQKKAELERV 162
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1442-1556 |
4.98e-04 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 44.72 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1442 QKAMDLDQDvlsalaEVEqlsKMVSEAKLRADEAKQSAEDILLKTNAT-------------KEKMDKSNEE-LRNLIKQI 1507
Cdd:CHL00094 497 QGASTLPKD------EVE---RMVKEAEKNAAEDKEKREKIDLKNQAEslcyqaekqlkelKDKISEEKKEkIENLIKKL 567
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 167614504 1508 RNFLTQDsaDLDSIEavanevlkmempSTPQQLQNLTEDIRERVESLSQ 1556
Cdd:CHL00094 568 RQALQND--NYESIK------------SLLEELQKALMEIGKEVYSSTS 602
|
|
| Alanine_zipper |
pfam11839 |
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane ... |
1569-1618 |
5.11e-04 |
|
Alanine-zipper, major outer membrane lipoprotein; This is a family of a major outer membrane lipoprotein, OprL that is an alanine-zipper. Zipper motifs are a seven-repeat motif where the first and fourth positions are occupied by an aliphatic residue, usually a leucine. These residues are positioned on the outside of the coil such as to bind firmly to one or more monomers of the protein to create a triple or five-helical coiled-coil that probably forms a seam in a membrane.
Pssm-ID: 432118 [Multi-domain] Cd Length: 69 Bit Score: 40.05 E-value: 5.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1569 ARAEMLLEEAKRASKSATDVKVTADmvkEALEEAEKAQVAAEKAIKQADE 1618
Cdd:pfam11839 8 SKADQAEQDAAAAQSAADSAKAKAD---EAAARANAAEAAAEEAQQAAEE 54
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1569-1768 |
5.39e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1569 ARAEMLLEEAKRASKSATDVKVTadmvkEALEEAEKAQVAAEKAI-----KQADEDIQGTQNlLTSIESETAASEETLFN 1643
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEA-----EAAAAAEKAAAAAEKEKaeeakRKAEEEAKRKAE-EERKAAEAEAAAKAEAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1644 ASQRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEMLQ 1723
Cdd:COG3064 156 AARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALA 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 167614504 1724 NEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEV 1768
Cdd:COG3064 236 AVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVV 280
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1456-1778 |
6.16e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDI--------LLKTNATKEKMDKSNEELRNLiKQIRNFLTQDSADLDSIEAVANe 1527
Cdd:PRK04863 851 RALADHESQEQQQRSQLEQAKEGLSALnrllprlnLLADETLADRVEEIREQLDEA-EEAKRFVQQHGNALAQLEPIVS- 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1528 VLKmempSTPQQLQNLTEDIRERVESLSQVEvilqhsaadiARAEMLLEEAKRA-----SKSATDVKVTADMV---KEAL 1599
Cdd:PRK04863 929 VLQ----SDPEQFEQLKQDYQQAQQTQRDAK----------QQAFALTEVVQRRahfsyEDAAEMLAKNSDLNeklRQRL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 EEAEKAQVAAEKAIKQADEdiQGTQN--LLTSIESETAASEETLfnasqriSELERNVEELKRKAAQNsgeAEyiekvvy 1677
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQA--QLAQYnqVLASLKSSYDAKRQML-------QELKQELQDLGVPADSG---AE------- 1055
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1678 tvKQSAEDvKKTLDGELDEKYKKVENLIAKKTEESADAR------RKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQ 1751
Cdd:PRK04863 1056 --ERARAR-RDELHARLSANRSRRNQLEKQLTFCEAEMDnltkklRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVER 1132
|
330 340
....*....|....*....|....*...
gi 167614504 1752 RYLedkAQELARLEG-EVRSllkdISQK 1778
Cdd:PRK04863 1133 RLH---RRELAYLSAdELRS----MSDK 1153
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1225-1562 |
6.42e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1225 RKVSEIKDILAQSPAAEPLKNIGNLFEEAEKLIKDVTEM---MAQVEVKLSDTTSQSNSTAKELDSLQTEAESLDNTVKE 1301
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAreeLEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1302 LAEQLEFIKN--SDIRGALDSITKYFQMSLEAEERVNASTTEPNSTV-EQSALMRDRVEDVMMERESQFKEKQEEQARLL 1378
Cdd:COG4372 99 AQEELESLQEeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1379 DELAGKLQSLDLSAAAEMTCGTPPGASCSETECGGPNCRTDEGERKCGGPgcGGLVTVAHNAWQKAMDLDQDVLSALAEV 1458
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE--AKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1459 EQLSKMVSEAKLRADEAKQSAEDILLK--------TNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIEAVANEVLK 1530
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALelealeeaALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|..
gi 167614504 1531 MEMPSTPQQLQNLTEDIRERVESLSQVEVILQ 1562
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1684-1778 |
6.96e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1684 EDVKKTLDGELDEKYKKVENLIAKKTEESADARRKAEML----QNEAKTL----LAQANSKLQLLKDLERKYEDNQryle 1755
Cdd:PRK07353 38 EDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAViaeaEAEADKLaaeaLAEAQAEAQASKEKARREIEQQ---- 113
|
90 100
....*....|....*....|...
gi 167614504 1756 dKAQELARLEGEVRSLLKDISQK 1778
Cdd:PRK07353 114 -KQAALAQLEQQVDALSRQILEK 135
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1546-1717 |
8.22e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1546 DIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQN 1625
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1626 LLtsieSETAASEETLFNAsqriselERNVEELKRKAAQNSGEAEYIEKvvyTVKQSAEDVKKTLDGELDEKYKKVENLI 1705
Cdd:pfam00529 132 LA----PIGGISRESLVTA-------GALVAQAQANLLATVAQLDQIYV---QITQSAAENQAEVRSELSGAQLQIAEAE 197
|
170
....*....|..
gi 167614504 1706 AKKTEESADARR 1717
Cdd:pfam00529 198 AELKLAKLDLER 209
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1457-1767 |
8.87e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1457 EVEQLSKMVSEAKLRADEAKQSAedillktnatkekmdkSNEELRNLIKQIrnfltqdsaDLDSIEAVAN-------EVL 1529
Cdd:PLN03229 437 EVEKLKEQILKAKESSSKPSELA----------------LNEMIEKLKKEI---------DLEYTEAVIAmglqerlENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1530 KMEMPSTPQQLQNLTEDIRERVESLSQvEVILQHSAA--------------DIARAEMLLEEAKRASKSATDV--KVTAD 1593
Cdd:PLN03229 492 REEFSKANSQDQLMHPVLMEKIEKLKD-EFNKRLSRApnylslkykldmlnEFSRAKALSEKKSKAEKLKAEInkKFKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1594 M----VKEALeEAEKAQVAAEKAIKQADEDiqgtQNLLTSIESetaASEETLFNASQRISELERNVEELKRKAAQNSGE- 1668
Cdd:PLN03229 571 MdrpeIKEKM-EALKAEVASSGASSGDELD----DDLKEKVEK---MKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQt 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1669 -----AEYIEKVVYTVKQSAEDVKKTLDGELDEKYKKVENLIAKKTEESADArRKAEMLQNEAKTLLAQANSKLQLLKDL 1743
Cdd:PLN03229 643 pppnlQEKIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEK-EKIEALEQQIKQKIAEALNSSELKEKF 721
|
330 340
....*....|....*....|....
gi 167614504 1744 ERKYEDNQRYLEDKAQELARLEGE 1767
Cdd:PLN03229 722 EELEAELAAARETAAESNGSLKND 745
|
|
| PhaP_Bmeg |
pfam09602 |
Polyhydroxyalkanoic acid inclusion protein (PhaP_Bmeg); This entry describes a protein found ... |
1251-1380 |
9.22e-04 |
|
Polyhydroxyalkanoic acid inclusion protein (PhaP_Bmeg); This entry describes a protein found in polyhydroxyalkanoic acid (PHA) gene regions and incorporated into PHA inclusions in Bacillus cereus and Bacillus megaterium. The role of the protein may include amino acid storage.
Pssm-ID: 370578 [Multi-domain] Cd Length: 168 Bit Score: 41.85 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1251 EEAEKLIKDVTEMMAQVEVKLSDTTSQ-SNSTAKELDSLQTEA-ESLDNTVKELAEQLEFIKNSDIRGALDSITKYFQMS 1328
Cdd:pfam09602 40 KQQQDLNQEFTKSLSSLERESKQTTSEiLGNLQKTVSNLASKNgNKDEDNISEWTDKLNEVSTKFEKLALSPSKSSFDLL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 167614504 1329 LEAEERVNASTTepnSTVEQSALMRDRVEDVMMERESQFKEKQEEQARLLDE 1380
Cdd:pfam09602 120 DQFEKQIEETSK---SFIEQQQKRRGEWQKVLEEYVEQAKDSQKNLAKRFEE 168
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1600-1727 |
1.19e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.67 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1600 EEAEKAQVAAEKAIKQadediqgtqnlltsIESETAASEETLFNASQRISELE---RNVEELKRKAAQNSGEAEY-IEKV 1675
Cdd:pfam20492 2 EEAEREKQELEERLKQ--------------YEEETKKAQEELEESEETAEELEeerRQAEEEAERLEQKRQEAEEeKERL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1676 vytvKQSAEDVKKT---LDGELDEKykkvENLIAKKTEESadaRRKAE---MLQNEAK 1727
Cdd:pfam20492 68 ----EESAEMEAEEkeqLEAELAEA----QEEIARLEEEV---ERKEEearRLQEELE 114
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1466-1765 |
1.20e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1466 SEAKLRADEAKQsAEDILLKTNATKEKMDKSNEELRNLIKQIRNfLTQDSADLDSIEAVA--NEVLKMEMPSTPQQLQNL 1543
Cdd:PLN02939 63 SKLQSNTDENGQ-LENTSLRTVMELPQKSTSSDDDHNRASMQRD-EAIAAIDNEQQTNSKdgEQLSDFQLEDLVGMIQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1544 TEDI----RERVESLSQVEVILQHSAA---DIARAEMLLEEAKRASKSATDVKVTADMVKEALEE--AEKAQVAAEKA-- 1612
Cdd:PLN02939 141 EKNIlllnQARLQALEDLEKILTEKEAlqgKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKlrNELLIRGATEGlc 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1613 ----------IKQADEDIQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRK--AAQNS-------------G 1667
Cdd:PLN02939 221 vhslskeldvLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKfiVAQEDvsklsplqydcwwE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1668 EAEYIEKVVYTVKQSAEDVKKTLDGElDEKYKKVENLIA--KKTEESADARRKAEMLQNEAKTLL-------AQANSKLQ 1738
Cdd:PLN02939 301 KVENLQDLLDRATNQVEKAALVLDQN-QDLRDKVDKLEAslKEANVSKFSSYKVELLQQKLKLLEerlqasdHEIHSYIQ 379
|
330 340
....*....|....*....|....*..
gi 167614504 1739 LLKDLERKYEDNQRYLEDKAQELARLE 1765
Cdd:PLN02939 380 LYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1547-1779 |
1.30e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1547 IRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDVKvtADMVKEALEEAEkaqvAAEKAIKQADEDIQgtqNL 1626
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK--QNKYDELVEEAK----TIKAEIEELTDELL---NL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1627 LTSIESETAAseetlfnasqrISELERNVEELKRKAAQNSGEAEYIEK--VVYTVKQ----------SAEDVKKTLDGEL 1694
Cdd:PHA02562 247 VMDIEDPSAA-----------LNKLNTAAAKIKSKIEQFQKVIKMYEKggVCPTCTQqisegpdritKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1695 DEKYKKVENLiAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKD 1774
Cdd:PHA02562 316 EKLDTAIDEL-EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
....*
gi 167614504 1775 ISQKV 1779
Cdd:PHA02562 395 KSELV 399
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1460-1767 |
1.39e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1460 QLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRNfltqdsadLDSIEAVANEVLKMEMPSTPQQ 1539
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRL--------LEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1540 LQNLTEDIRERVESLSQVEVIlqhsaadiarAEMLLEEAKRASKSATDVKVTADMVKEALEEAEKAQvaaeKAIKQADED 1619
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADA----------REVISCLKNELSELRRQIQRAELELQSTNSELEELQ----ERLDLLKAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1620 IQGTQNLLTSIEsetaASEETLFNASQRISELERNVE------------------------ELKRKAAQNSGEAEYIEKV 1675
Cdd:pfam05557 148 ASEAEQLRQNLE----KQQSSLAEAEQRIKELEFEIQsqeqdseivknskselaripelekELERLREHNKHLNENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1676 VyTVKQSAEDVKKTLDGEldEKYK--------KVENLIAK-----KTEESA--------DARRKAEMLQNEAKTLLAQAN 1734
Cdd:pfam05557 224 L-LLKEEVEDLKRKLERE--EKYReeaatlelEKEKLEQElqswvKLAQDTglnlrspeDLSRRIEQLQQREIVLKEENS 300
|
330 340 350
....*....|....*....|....*....|....
gi 167614504 1735 SKLQLLKDLERkyedNQRYLEDK-AQELARLEGE 1767
Cdd:pfam05557 301 SLTSSARQLEK----ARRELEQElAQYLKKIEDL 330
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1201-1390 |
1.43e-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: 43.51 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1201 LEKAKALKISGVIGPYRETVDSVERKVSEIKDILAQspAAEPLKNIGNLFEEAEKLIKDVTEMMAQVEVKLSDTTSQSNS 1280
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE--LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1281 TAKELDSLQTEA-------ESLDNTVKELAEQLEFIKNS------DIRGALDSITKYFQMSLEAEERVNASTTEPNSTVE 1347
Cdd:TIGR02168 808 LRAELTLLNEEAanlrerlESLERRIAATERRLEDLEEQieelseDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 167614504 1348 QSALMRDRVEDVMMERESQFKEKQEEQaRLLDELAGKLQSLDL 1390
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELR-RELEELREKLAQLEL 929
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1630-1784 |
1.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1630 IESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIE---KVVYTVKQ--SAEDVKKTLD------GELDEKY 1698
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeiDVASAEREiaELEAELERLDassddlAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1699 KKVENLIAKKTEESADARRKAEMLQNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLEGEVRSLLKDISQK 1778
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
....*.
gi 167614504 1779 VAVYST 1784
Cdd:COG4913 775 IDALRA 780
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
917-966 |
1.63e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.06 E-value: 1.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 167614504 917 CPCpdgpDSGRQFARSCyqDPVTLQlaCVCDPGYIGSRCDDCASGYFGNP 966
Cdd:smart00180 1 CDC----DPGGSASGTC--DPDTGQ--CECKPNVTGRRCDRCAPGYYGDG 42
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
1564-1680 |
1.67e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 40.93 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1564 SAADIARAEM---------LLEEAkRASKSAtdvkvtadMVKEALEEAEK--------AQVAAEKAIKQADEDIQGTQN- 1625
Cdd:PRK14471 49 ASAEEARKEMqnlqadnerLLKEA-RAERDA--------ILKEAREIKEKmiadakeeAQVEGDKMIEQAKASIESEKNa 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 1626 LLTSIESETAaseetlfNASQRISE-LERnvEELKRKAAQnsgeAEYIEKVVYTVK 1680
Cdd:PRK14471 120 AMAEIKNQVA-------NLSVEIAEkVLR--KELSNKEKQ----HKLVEKMLGDVK 162
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
1540-1636 |
1.79e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 40.37 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1540 LQNLTEDIRERVES-LSQVEVILQHSAADIARAEMLLEEAK-RASKSATDVKVTADMVKEALEEAekAQVAAEKAIKQAD 1617
Cdd:pfam00430 24 LGKVLDKRRELIADeIAEAEERRKDAAAALAEAEQQLKEARaEAQEIIENAKKRAEKLKEEIVAA--AEAEAERIIEQAA 101
|
90 100
....*....|....*....|
gi 167614504 1618 EDI-QGTQNLLTSIESETAA 1636
Cdd:pfam00430 102 AEIeQEKDRALAELRQQVVA 121
|
|
| PhaF |
COG3937 |
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport ... |
1568-1661 |
1.88e-03 |
|
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms];
Pssm-ID: 443138 [Multi-domain] Cd Length: 103 Bit Score: 39.40 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1568 IARAEMLLEEAKRasksatdvkvtadMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTsiesetaASE-ETLfnaSQ 1646
Cdd:COG3937 31 VEKGELTEEEAKK-------------FVDELVEKGEEEKEELEEKIEEQVEEALEKLGLAT-------KEEvDEL---EE 87
|
90
....*....|....*
gi 167614504 1647 RISELERNVEELKRK 1661
Cdd:COG3937 88 RIDRLEKQLRELENK 102
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
271-326 |
1.94e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 37.72 E-value: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 271 CFCYGHASECAPVDgfneevegMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEG 326
Cdd:pfam00053 1 CDCNPHGSLSDTCD--------PETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1469-1778 |
1.94e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1469 KLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLIKQIRnfLTQDSADLDSIEA-VANEVLKMEMPSTPQQLQNLTeDI 1547
Cdd:PTZ00440 1477 EKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPN--IKREGDVLNNDKStIAYETIQYNLGRVKHNLLNIL-NI 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1548 RERVESLSQVEVILQHSAADIAR--AEMLLEEAKraSKSATDVKVTADMVKEaleeaEKAQVAAEKAIKQADEDIQGTQN 1625
Cdd:PTZ00440 1554 KDEIETILNKAQDLMRDISKISKivENKNLENLN--DKEADYVKYLDNILKE-----KQLMEAEYKKLNEIYSDVDNIEK 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1626 LLTS--IESETAASEETLFNASQRISELERNVEELKRKAAQNSG--EAEYIEKvvYTVKQSAEDVKKTLD---GELDEKY 1698
Cdd:PTZ00440 1627 ELKKhkKNYEIGLLEKVIEINKNIKLYMDSTKESLNSLVNNFSSlfNNFYLNK--YNINENLEKYKKKLNeiyNEFMESY 1704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1699 KKVENLIAKKTEESADArrkaemlqNEAKTLLAQANSKlqlLKDLERKYEDNQRYLED-KAQELARLEGEVRSLLKDISQ 1777
Cdd:PTZ00440 1705 NIIQEKMKEVSNDDVDY--------NEAKTLREEAQKE---EVNLNNKEEEAKKYLNDiKKQESFRFILYMKEKLDELSK 1773
|
.
gi 167614504 1778 K 1778
Cdd:PTZ00440 1774 M 1774
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
1679-1747 |
1.99e-03 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 39.10 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1679 VKQSAEdvKKTLDGELDEKYKKVENL----------IAKKTEESADARRKAEMLQNEAKTL---LAQANSKLQLLKDLER 1745
Cdd:pfam08647 6 VKLEQA--FEELSEQLDKKVKDLTILeekklrleaeKAKADQKYFAAMRSKDALENENKKLntlLSKSSELIEQLKETEK 83
|
..
gi 167614504 1746 KY 1747
Cdd:pfam08647 84 EF 85
|
|
| Prefoldin_alpha_GimC |
cd23160 |
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric ... |
1538-1657 |
2.05e-03 |
|
Prefoldin alpha subunit, archaeal; Archaeal alpha subunit of prefoldin (GimC), a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467476 [Multi-domain] Cd Length: 127 Bit Score: 40.16 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSaTDVKV--TAD-MVKEALEEAEK------AQVA 1608
Cdd:cd23160 3 QRLLAELQQLEQQAEALQQQIELLQASINELNRAKETLEELKKLKEG-TEILVpiGGGsFVKAKIKDTDKvlvnigAGVV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 167614504 1609 AEKAIKQADEDIqgtQNLLTSIESETAASEETLFNASQRISELERNVEE 1657
Cdd:cd23160 82 VEKTIDEAIEIL---EKRIKELEKALEKLQEQLQQIAQRLEELEAELQE 127
|
|
| PLU-1 |
pfam08429 |
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. ... |
1455-1618 |
2.32e-03 |
|
PLU-1-like protein; Sequences in this family bear similarity to the central region of PLU-1. This is a nuclear protein that may have a role in DNA-binding and transcription, and is closely associated with the malignant phenotype of breast cancer. This region is found in various other Jumonji/ARID domain-containing proteins (see pfam02373, pfam01388).
Pssm-ID: 462475 [Multi-domain] Cd Length: 336 Bit Score: 42.20 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1455 LAEVEQLSKMVSEAK-LraDEAKQsaedillktnaTKEKMDKSNEELRNLIKQ-IRNFLTQDSADL-----------DSI 1521
Cdd:pfam08429 151 LPELEELEKVLEQLKwL--EEVRE-----------TSRKKSLTLEDVRELIEEgVELGIPPPYEDLmaelqelltagERW 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1522 EAVANEVLKMEMPStPQQLQNLTEDIRE---RVESLSQVEVILQHSAADIARAEMLLE---EAKRAsksatdvkvTADMV 1595
Cdd:pfam08429 218 EEKAKELLSRERVS-LAQLEALSKEAQEipvSLPNLAALDEILKKAREWQRQIEALYQrsdFGKRP---------TLDEL 287
|
170 180
....*....|....*....|....*....
gi 167614504 1596 KEALEEAEKAQV------AAEKAIKQADE 1618
Cdd:pfam08429 288 EELLAKGESLPVkpeglsDLEKEVKRAED 316
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1602-1781 |
2.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1602 AEKAQVAAEKAIKQADEdiQGTQNLLTSIESETAASEETLFNASQRISELERNVEELKRKAAQNSGEAEYIEKvvytvkq 1681
Cdd:PRK12705 32 AKEAERILQEAQKEAEE--KLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDN------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1682 sAEDVKKTLDGELDEKYKKVENLiakkteesadARRKAEMLQNEAKTLLAQANSklQLLKDLERKYEdnqrylEDKAQEL 1761
Cdd:PRK12705 103 -LENQLEEREKALSARELELEEL----------EKQLDNELYRVAGLTPEQARK--LLLKLLDAELE------EEKAQRV 163
|
170 180
....*....|....*....|
gi 167614504 1762 ARLEGEVRSLLKDISQKVAV 1781
Cdd:PRK12705 164 KKIEEEADLEAERKAQNILA 183
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1632-1759 |
2.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1632 SETAASEETLFNASQRISELERNVEELKRKAAQNSGEA--------EYIEKvVYTVKQSAEDVKKtldgELDEKYKKVEN 1703
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELkelaekrdELNAQ-VKELREEAQELRE----KRDELNEKVKE 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 167614504 1704 LIAKKTEESADARRKAEMLqNEAKTLLAQANSKLQLLKDLERKYEDnqryLEDKAQ 1759
Cdd:COG1340 76 LKEERDELNEKLNELREEL-DELRKELAELNKAGGSIDKLRKEIER----LEWRQQ 126
|
|
| GARP |
pfam16731 |
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, ... |
1447-1612 |
2.74e-03 |
|
Glutamic acid/alanine-rich protein of Trypanosoma; GARP, or glutamic acid/alanine-rich protein, is one of a subset of major surface molecules on Trypanosoma species. They are all surface-orientated, immunodominant, and highly charged. GARP is interesting as ts expression coincides with the loss and gain of variant surface glycoprotein (VSG) molecules in the tsetse vector. It has an extended helical bundle structure that is homologous to the core surface structure of VSG, suggesting that it might replace the bloodstream VSG as the trypanosomes differentiate inside the tsetse vector after a blood-meal.
Pssm-ID: 435545 [Multi-domain] Cd Length: 192 Bit Score: 40.82 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1447 LDQDVLSALAEVEQLSKMVSEAKLRADEAKQSAEDILLKTNATKEKMDKSNEELRNLI-------KQIRNfLTQDSADLD 1519
Cdd:pfam16731 16 LPDTVSSALETAAAASSKAFKAKVQAEEAVELAESAGLNDPKAKEAVTRAREAAVRATeaaeaaaTAASN-VEINAANLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1520 SIEAVANEVLKMEMPSTPQQlQNLTEDIRE------------RVESLSQ-VEVILQHSAADIARAemLLEEAKRASKSat 1586
Cdd:pfam16731 95 SVAWAYVPSLDDGLKKLAEC-GNADEDVREaakkctktaenvTAQSLTEaLEGLRKLFDVKSAER--LRKETVEAHEE-- 169
|
170 180
....*....|....*....|....*.
gi 167614504 1587 dvkvtADMVKEALEEAEKAQVAAEKA 1612
Cdd:pfam16731 170 -----LKSLEKAVEEAVRAQKAAEDA 190
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1473-1619 |
2.75e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1473 DEAKQSAEDI---LLKTNATKEKMDKSNEELRNLIKQIRNFLTQDSADLDSIeavaNEVLKM-----EMPSTPQQLqnlt 1544
Cdd:PHA02562 223 DELVEEAKTIkaeIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF----QKVIKMyekggVCPTCTQQI---- 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1545 EDIRERVESLSQVEVILQHS--AADIARAEM--LLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADED 1619
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSleKLDTAIDELeeIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
|
| alph_xenorhab_B |
NF033927 |
alpha-xenorhabdolysin family binary toxin subunit B; |
1498-1732 |
2.76e-03 |
|
alpha-xenorhabdolysin family binary toxin subunit B;
Pssm-ID: 411488 [Multi-domain] Cd Length: 223 Bit Score: 41.08 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1498 EELRNLIKQIRNfltqdsadldSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEE 1577
Cdd:NF033927 7 AALRKSAAKIAN----------KLDDLSQINLREATLDLLAQLQEQIAELEAQIAALESKLNELAEDRKVIIEAIDLIEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1578 AKrasksatdvkvTADMVKEAL---EEAEKAQVA-AEKAI-KQAdedIQGTQNLLTSIE-----SETAASEETLfnaSQR 1647
Cdd:NF033927 77 YN-----------IADLFKDLLptaEEIDSLGLPpPEKDLvKAA---IERLKKLLGKISegltyIDLVEARDKL---RDR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1648 ISELERNVEELKRKAAQNSGEAEYIEKVvytvkQSAEDVKKTLDGEldekYKKVEN----LIAKKTEESADarrkaEMLQ 1723
Cdd:NF033927 140 INALLAESRTLDKDIKALAGKLEELTAI-----AAIDEERATWVAE----ARKVEQawesFLDQLTELTSD-----SANL 205
|
....*....
gi 167614504 1724 NEAKTLLAQ 1732
Cdd:NF033927 206 AQLITQLNG 214
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1669-1775 |
2.78e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1669 AEYIEKVvytvkQSAEDVKKTLDGELDEKYKKVENLIAKKTE----ESADARRKAEMLQNEAKTLLAQANSKLQLLKDLE 1744
Cdd:pfam00038 14 ASYIDKV-----RFLEQQNKLLETKISELRQKKGAEPSRLYSlyekEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 167614504 1745 RKYED--NQRY-LEDKAQELAR-----------LEGEVRSLLKDI 1775
Cdd:pfam00038 89 QKYEDelNLRTsAENDLVGLRKdldeatlarvdLEAKIESLKEEL 133
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1548-1666 |
2.90e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 39.54 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1548 RERVESLSQVEVILQHSAADIARAEMLLEEAKRASKSATDV--KVTADMVK--EALEE--AEKAQVAAEKA-IKQADEDI 1620
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAqqNYERELVLhaEDIKAlqALREELNELKAeIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 167614504 1621 QGTQNLLTSIESETAASEETLfnaSQRISELERNVEELKrkaAQNS 1666
Cdd:pfam07926 81 ESAKAELEESEESWEEQKKEL---EKELSELEKRIEDLN---EQNK 120
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1688-1773 |
3.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1688 KTLDGELDEKykkVENLIAKKTEESADARRKAEmlqnEAKTLLAQANsklQLLKDLERKYEDNQrylEDKAQELARLEGE 1767
Cdd:PRK00409 508 KKLIGEDKEK---LNELIASLEELERELEQKAE----EAEALLKEAE---KLKEELEEKKEKLQ---EEEDKLLEEAEKE 574
|
....*.
gi 167614504 1768 VRSLLK 1773
Cdd:PRK00409 575 AQQAIK 580
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
1538-1664 |
3.23e-03 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 40.63 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQ-LQNLTEDIRERVESLSQVEVILQHSAADiaraemlleeAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQA 1616
Cdd:pfam05335 58 QQiVEQLEQELREAEAVVQEESASLQQSQAN----------ANAAQRAAQQAQQQLEALTAALKAAQANLENAEQVAAGA 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 167614504 1617 DEDIQGTQNLLTsiesetaaseetlfNASQRISELERNVEELK------RKAAQ 1664
Cdd:pfam05335 128 QQELAEKTQLLE--------------AAKKRVERLQRQLAEARadlektKKAAY 167
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1456-1657 |
3.58e-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: 41.06 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1456 AEVEQLSKMVSEAKLRADEAKQSAEDIllktnatkekmDKSNEELRNLIKQIRNFLTQDSADLDSIeavanevlkmempS 1535
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDL-----------EKEIKRLELEIEEVEARIKKYEEQLGNV-------------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 TPQQLQNLTEDIrervESLsqvevilqhsAADIARAEMLLEEakrasksatdvkvtadmVKEALEEAEKAQVAAEKAIKQ 1615
Cdd:COG1579 87 NNKEYEALQKEI----ESL----------KRRISDLEDEILE-----------------LMERIEELEEELAELEAELAE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 167614504 1616 ADEDIQGTQNLLTSIESETAASEETLfnaSQRISELERNVEE 1657
Cdd:COG1579 136 LEAELEEKKAELDEELAELEAELEEL---EAEREELAAKIPP 174
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1538-1777 |
3.71e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1538 QQLQNLteDIRERVESLSQVEVILQhsaadiarAEMLLEEAKRASKSATDVKVTAdmVKEALEEAEKAQ-----VAAEKA 1612
Cdd:PRK04778 39 QELENL--PVNDELEKVKKLNLTGQ--------SEEKFEEWRQKWDEIVTNSLPD--IEEQLFEAEELNdkfrfRKAKHE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1613 IKQADEDIQGTQNLLTSIESEtaaseetlfnasqriselernVEELKRKAAQNSGEAEyiekvvyTVKQSAEDVKKTLDG 1692
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEE---------------------LQELLESEEKNREEVE-------QLKDLYRELRKSLLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1693 ----------ELDEKYKKVENLIAKKTEESAD-----ARR-----KAEMLQNEAKT-----LLAQANSKL-QLLKDLE-- 1744
Cdd:PRK04778 159 nrfsfgpaldELEKQLENLEEEFSQFVELTESgdyveAREildqlEEELAALEQIMeeipeLLKELQTELpDQLQELKag 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 167614504 1745 -RKYEDNQRYLEDKA--QELARLEGEVRSLLKDISQ 1777
Cdd:PRK04778 239 yRELVEEGYHLDHLDieKEIQDLKEQIDENLALLEE 274
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1589-1711 |
4.42e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 40.31 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1589 KVTADMVKEALEEAEK----AQVAAEKAIKQADEDIqgtQNLLTSIESETAASEETLFNasQRISELERnveELKRK--A 1662
Cdd:COG1390 6 KIIEEILEEAEAEAEEileeAEEEAEKILEEAEEEA---EEIKEEILEKAEREAEREKR--RIISSAEL---EARKEllE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 167614504 1663 AQNsgeaEYIEKVVYTVKQSAEDVKKtldgelDEKYKK-VENLIAKKTEE 1711
Cdd:COG1390 78 AKE----ELIEEVFEEALEKLKNLPK------DPEYKElLKKLLKEAAEE 117
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
1646-1741 |
5.25e-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: 38.68 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1646 QRISELERNVEELKRKAAQNSGEAEYIEKVVYTVKQSAEDVKKtldgeldEKYKKVENLIakkteesADARRKAEMLQNE 1725
Cdd:COG3599 41 RENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAEEVKE-------NAEKEAELII-------KEAELEAEKIIEE 106
|
90
....*....|....*.
gi 167614504 1726 AKTLLAQANSKLQLLK 1741
Cdd:COG3599 107 AQEKARKIVREIEELK 122
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1461-1672 |
5.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1461 LSKMVSEAKLRadEAKQSAEDILLKTNA-----TKEKMDKSNEElrnlIKQIRNFLTQDSADLDsieavaNEVLKMEmps 1535
Cdd:PRK12704 24 VRKKIAEAKIK--EAEEEAKRILEEAKKeaeaiKKEALLEAKEE----IHKLRNEFEKELRERR------NELQKLE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1536 tpQQLQNLTEDIRERVESLSQVEVILQHSAADIARAEMLLEEAKrasksatdvKVTADMVKEALEEAEK-AQVAAEKAIK 1614
Cdd:PRK12704 89 --KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE---------EELEELIEEQLQELERiSGLTAEEAKE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 167614504 1615 QadediqgtqnLLTSIESEtaASEEtlfnASQRISELErnvEELKRKAAQnsgEAEYI 1672
Cdd:PRK12704 158 I----------LLEKVEEE--ARHE----AAVLIKEIE---EEAKEEADK---KAKEI 193
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1693-1778 |
6.58e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1693 ELDEKYKKVENLIAKKTEESADARRKAEML-------QNEAKTLLAQANSKLQLLKDLERKYEDNQRYLEDKAQELARLE 1765
Cdd:pfam20492 10 ELEERLKQYEEETKKAQEELEESEETAEELeeerrqaEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQ 89
|
90
....*....|...
gi 167614504 1766 GEVrSLLKDISQK 1778
Cdd:pfam20492 90 EEI-ARLEEEVER 101
|
|
| PLC-beta_C |
pfam08703 |
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of ... |
1631-1773 |
9.37e-03 |
|
PLC-beta C terminal; This domain corresponds to the alpha helical C terminal domain of phospholipase C beta.
Pssm-ID: 462571 [Multi-domain] Cd Length: 176 Bit Score: 38.89 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614504 1631 ESETAASEETLFNASQRISEL--ERNVEELKRKAAQNSGEAEYIEKVVYT--VKQSAEDVKKTLDGELDEKYKKVENliA 1706
Cdd:pfam08703 23 EQEKKRKEQHLTEQIQKLKELarEKQAAELKALKESSESEKKEMKKKLERkrLESIQEAKKRTSDKAAQERLKKEIN--N 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614504 1707 KKTEESADARRKAEMLQ--NEAKTLLAQANSkLQLLKDLERKYEdnQRYLEDKAQELARLEGEVRSLLK 1773
Cdd:pfam08703 101 SHIQEVVQSIKQLEEKQkrRQEKLEEKQAEC-LQQIKEEEPQLQ--AELNAEYEEKLKGLPAEVRESVK 166
|
|
| |
